Loading…
The Binding Specificity of OppA Determines the Selectivity of the Oligopeptide ATP-binding Cassette Transporter
The purification and functional reconstitution of a five-component oligopeptide ATP-binding cassette transporter with a remarkably wide substrate specificity are described. High-affinity peptide uptake was dependent on liganded substrate-binding protein OppA, which interacts with the translocator Op...
Saved in:
| Published in: | The Journal of biological chemistry 2004-07, Vol.279 (31), p.32301-32307 |
|---|---|
| Main Authors: | , , , |
| Format: | Article |
| Language: | English |
| Subjects: | |
| Citations: | Items that this one cites Items that cite this one |
| Online Access: | Get full text |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| cited_by | cdi_FETCH-LOGICAL-c358t-f723a4eb61bdba8f1a905ce61e64ecb66e6f21ca03a29587b50b50be3a0e64083 |
|---|---|
| cites | cdi_FETCH-LOGICAL-c358t-f723a4eb61bdba8f1a905ce61e64ecb66e6f21ca03a29587b50b50be3a0e64083 |
| container_end_page | 32307 |
| container_issue | 31 |
| container_start_page | 32301 |
| container_title | The Journal of biological chemistry |
| container_volume | 279 |
| creator | Doeven, Mark K Abele, Rupert Tampé, Robert Poolman, Bert |
| description | The purification and functional reconstitution of a five-component oligopeptide ATP-binding cassette transporter with a remarkably
wide substrate specificity are described. High-affinity peptide uptake was dependent on liganded substrate-binding protein
OppA, which interacts with the translocator OppBCDF with higher affinity than unliganded OppA. Transport screening with combinatorial
peptide libraries revealed that (i) the Opp transporter is not selective with respect to amino acid side chains of the transported
peptides; (ii) any peptide that can bind to OppA is transported via Opp, including very long peptides up to 35 residues long;
and (iii) the binding specificity of OppA largely determines the overall transport selectivity. |
| doi_str_mv | 10.1074/jbc.M404343200 |
| format | article |
| fullrecord | <record><control><sourceid>pubmed_cross</sourceid><recordid>TN_cdi_crossref_primary_10_1074_jbc_M404343200</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>15169767</sourcerecordid><originalsourceid>FETCH-LOGICAL-c358t-f723a4eb61bdba8f1a905ce61e64ecb66e6f21ca03a29587b50b50be3a0e64083</originalsourceid><addsrcrecordid>eNpFkE1Lw0AQhhdRbK1ePUoOXlP3I9kkx1o_oVKhEbwtu5tJs6VNluyq9N-7pYEOAwPD876HB6FbgqcEZ8nDRunpR4ITljCK8RkaE5yzmKXk-xyNMaYkLmiaj9CVcxscJinIJRqRlPAi49kYdWUD0aNpK9Ouo5UFbWqjjd9HXR0trZ1FT-Ch35kWXOQDuoItaG9-B-TwWm7NurNgvakgmpWfsRrq5tI58B6ispets10fmq7RRS23Dm6GO0FfL8_l_C1eLF_f57NFrFma-7jOKJMJKE5UpWReE1ngVAMnwBPQinPgNSVaYiZpkeaZSvFhgUkciKBggqbHXt13zvVQC9ubnez3gmBxMCeCOXEyFwJ3x4D9UTuoTvigKgD3R6Ax6-bP9CCU6XQDO0GzQjAiGGWYsH-uJncT</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype></control><display><type>article</type><title>The Binding Specificity of OppA Determines the Selectivity of the Oligopeptide ATP-binding Cassette Transporter</title><source>ScienceDirect Journals</source><creator>Doeven, Mark K ; Abele, Rupert ; Tampé, Robert ; Poolman, Bert</creator><creatorcontrib>Doeven, Mark K ; Abele, Rupert ; Tampé, Robert ; Poolman, Bert</creatorcontrib><description>The purification and functional reconstitution of a five-component oligopeptide ATP-binding cassette transporter with a remarkably
wide substrate specificity are described. High-affinity peptide uptake was dependent on liganded substrate-binding protein
OppA, which interacts with the translocator OppBCDF with higher affinity than unliganded OppA. Transport screening with combinatorial
peptide libraries revealed that (i) the Opp transporter is not selective with respect to amino acid side chains of the transported
peptides; (ii) any peptide that can bind to OppA is transported via Opp, including very long peptides up to 35 residues long;
and (iii) the binding specificity of OppA largely determines the overall transport selectivity.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.M404343200</identifier><identifier>PMID: 15169767</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>Adenosine Triphosphate - metabolism ; Amino Acids - chemistry ; Bacterial Proteins ; Biological Transport ; Bradykinin - pharmacokinetics ; Carrier Proteins - chemistry ; Carrier Proteins - metabolism ; Cell Membrane - metabolism ; Dose-Response Relationship, Drug ; Immunoblotting ; Lactococcus lactis - metabolism ; Lipoproteins - chemistry ; Lipoproteins - metabolism ; Methionine - chemistry ; Oligopeptides - chemistry ; Peptide Library ; Peptides - chemistry ; Plasmids - metabolism ; Protein Binding ; Protein Structure, Tertiary ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization ; Time Factors ; Valine - chemistry</subject><ispartof>The Journal of biological chemistry, 2004-07, Vol.279 (31), p.32301-32307</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c358t-f723a4eb61bdba8f1a905ce61e64ecb66e6f21ca03a29587b50b50be3a0e64083</citedby><cites>FETCH-LOGICAL-c358t-f723a4eb61bdba8f1a905ce61e64ecb66e6f21ca03a29587b50b50be3a0e64083</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15169767$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Doeven, Mark K</creatorcontrib><creatorcontrib>Abele, Rupert</creatorcontrib><creatorcontrib>Tampé, Robert</creatorcontrib><creatorcontrib>Poolman, Bert</creatorcontrib><title>The Binding Specificity of OppA Determines the Selectivity of the Oligopeptide ATP-binding Cassette Transporter</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>The purification and functional reconstitution of a five-component oligopeptide ATP-binding cassette transporter with a remarkably
wide substrate specificity are described. High-affinity peptide uptake was dependent on liganded substrate-binding protein
OppA, which interacts with the translocator OppBCDF with higher affinity than unliganded OppA. Transport screening with combinatorial
peptide libraries revealed that (i) the Opp transporter is not selective with respect to amino acid side chains of the transported
peptides; (ii) any peptide that can bind to OppA is transported via Opp, including very long peptides up to 35 residues long;
and (iii) the binding specificity of OppA largely determines the overall transport selectivity.</description><subject>Adenosine Triphosphate - metabolism</subject><subject>Amino Acids - chemistry</subject><subject>Bacterial Proteins</subject><subject>Biological Transport</subject><subject>Bradykinin - pharmacokinetics</subject><subject>Carrier Proteins - chemistry</subject><subject>Carrier Proteins - metabolism</subject><subject>Cell Membrane - metabolism</subject><subject>Dose-Response Relationship, Drug</subject><subject>Immunoblotting</subject><subject>Lactococcus lactis - metabolism</subject><subject>Lipoproteins - chemistry</subject><subject>Lipoproteins - metabolism</subject><subject>Methionine - chemistry</subject><subject>Oligopeptides - chemistry</subject><subject>Peptide Library</subject><subject>Peptides - chemistry</subject><subject>Plasmids - metabolism</subject><subject>Protein Binding</subject><subject>Protein Structure, Tertiary</subject><subject>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</subject><subject>Time Factors</subject><subject>Valine - chemistry</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><recordid>eNpFkE1Lw0AQhhdRbK1ePUoOXlP3I9kkx1o_oVKhEbwtu5tJs6VNluyq9N-7pYEOAwPD876HB6FbgqcEZ8nDRunpR4ITljCK8RkaE5yzmKXk-xyNMaYkLmiaj9CVcxscJinIJRqRlPAi49kYdWUD0aNpK9Ouo5UFbWqjjd9HXR0trZ1FT-Ch35kWXOQDuoItaG9-B-TwWm7NurNgvakgmpWfsRrq5tI58B6ispets10fmq7RRS23Dm6GO0FfL8_l_C1eLF_f57NFrFma-7jOKJMJKE5UpWReE1ngVAMnwBPQinPgNSVaYiZpkeaZSvFhgUkciKBggqbHXt13zvVQC9ubnez3gmBxMCeCOXEyFwJ3x4D9UTuoTvigKgD3R6Ax6-bP9CCU6XQDO0GzQjAiGGWYsH-uJncT</recordid><startdate>20040730</startdate><enddate>20040730</enddate><creator>Doeven, Mark K</creator><creator>Abele, Rupert</creator><creator>Tampé, Robert</creator><creator>Poolman, Bert</creator><general>American Society for Biochemistry and Molecular Biology</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope></search><sort><creationdate>20040730</creationdate><title>The Binding Specificity of OppA Determines the Selectivity of the Oligopeptide ATP-binding Cassette Transporter</title><author>Doeven, Mark K ; Abele, Rupert ; Tampé, Robert ; Poolman, Bert</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c358t-f723a4eb61bdba8f1a905ce61e64ecb66e6f21ca03a29587b50b50be3a0e64083</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Adenosine Triphosphate - metabolism</topic><topic>Amino Acids - chemistry</topic><topic>Bacterial Proteins</topic><topic>Biological Transport</topic><topic>Bradykinin - pharmacokinetics</topic><topic>Carrier Proteins - chemistry</topic><topic>Carrier Proteins - metabolism</topic><topic>Cell Membrane - metabolism</topic><topic>Dose-Response Relationship, Drug</topic><topic>Immunoblotting</topic><topic>Lactococcus lactis - metabolism</topic><topic>Lipoproteins - chemistry</topic><topic>Lipoproteins - metabolism</topic><topic>Methionine - chemistry</topic><topic>Oligopeptides - chemistry</topic><topic>Peptide Library</topic><topic>Peptides - chemistry</topic><topic>Plasmids - metabolism</topic><topic>Protein Binding</topic><topic>Protein Structure, Tertiary</topic><topic>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</topic><topic>Time Factors</topic><topic>Valine - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Doeven, Mark K</creatorcontrib><creatorcontrib>Abele, Rupert</creatorcontrib><creatorcontrib>Tampé, Robert</creatorcontrib><creatorcontrib>Poolman, Bert</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Doeven, Mark K</au><au>Abele, Rupert</au><au>Tampé, Robert</au><au>Poolman, Bert</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The Binding Specificity of OppA Determines the Selectivity of the Oligopeptide ATP-binding Cassette Transporter</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>2004-07-30</date><risdate>2004</risdate><volume>279</volume><issue>31</issue><spage>32301</spage><epage>32307</epage><pages>32301-32307</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>The purification and functional reconstitution of a five-component oligopeptide ATP-binding cassette transporter with a remarkably
wide substrate specificity are described. High-affinity peptide uptake was dependent on liganded substrate-binding protein
OppA, which interacts with the translocator OppBCDF with higher affinity than unliganded OppA. Transport screening with combinatorial
peptide libraries revealed that (i) the Opp transporter is not selective with respect to amino acid side chains of the transported
peptides; (ii) any peptide that can bind to OppA is transported via Opp, including very long peptides up to 35 residues long;
and (iii) the binding specificity of OppA largely determines the overall transport selectivity.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>15169767</pmid><doi>10.1074/jbc.M404343200</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0021-9258 |
| ispartof | The Journal of biological chemistry, 2004-07, Vol.279 (31), p.32301-32307 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_crossref_primary_10_1074_jbc_M404343200 |
| source | ScienceDirect Journals |
| subjects | Adenosine Triphosphate - metabolism Amino Acids - chemistry Bacterial Proteins Biological Transport Bradykinin - pharmacokinetics Carrier Proteins - chemistry Carrier Proteins - metabolism Cell Membrane - metabolism Dose-Response Relationship, Drug Immunoblotting Lactococcus lactis - metabolism Lipoproteins - chemistry Lipoproteins - metabolism Methionine - chemistry Oligopeptides - chemistry Peptide Library Peptides - chemistry Plasmids - metabolism Protein Binding Protein Structure, Tertiary Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization Time Factors Valine - chemistry |
| title | The Binding Specificity of OppA Determines the Selectivity of the Oligopeptide ATP-binding Cassette Transporter |
| url | http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-01T13%3A50%3A47IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-pubmed_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=The%20Binding%20Specificity%20of%20OppA%20Determines%20the%20Selectivity%20of%20the%20Oligopeptide%20ATP-binding%20Cassette%20Transporter&rft.jtitle=The%20Journal%20of%20biological%20chemistry&rft.au=Doeven,%20Mark%20K&rft.date=2004-07-30&rft.volume=279&rft.issue=31&rft.spage=32301&rft.epage=32307&rft.pages=32301-32307&rft.issn=0021-9258&rft.eissn=1083-351X&rft_id=info:doi/10.1074/jbc.M404343200&rft_dat=%3Cpubmed_cross%3E15169767%3C/pubmed_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c358t-f723a4eb61bdba8f1a905ce61e64ecb66e6f21ca03a29587b50b50be3a0e64083%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_id=info:pmid/15169767&rfr_iscdi=true |