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The importance of the conserved Arg191–Asp227 salt bridge of triosephosphate isomerase for folding, stability, and catalysis
Triosephosphate isomerase (TIM) has a conserved salt bridge 20 Å away from both the active site and the dimer interface. In this study, four salt bridge mutants of Trypanosoma brucei brucei TIM were characterized. The folding and stability of the mutants are impaired compared to the wild-type enzyme...
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Published in: | FEBS letters 2002-05, Vol.518 (1), p.39-42 |
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creator | Kursula, Inari Partanen, Sanna Lambeir, Anne-Marie Wierenga, Rik K. |
description | Triosephosphate isomerase (TIM) has a conserved salt bridge 20 Å away from both the active site and the dimer interface. In this study, four salt bridge mutants of
Trypanosoma brucei brucei TIM were characterized. The folding and stability of the mutants are impaired compared to the wild-type enzyme. This salt bridge is part of a hydrogen bonding network which tethers the C-terminal β7α7β8α8 unit to the bulk of the protein. In the variants D227N, D227A, and R191S, this network is preserved, as can be deduced from the structure of the R191S variant. In the R191A variant, the side chain at position 191 cannot contribute to this network. Also the catalytic power of this variant is most affected. |
doi_str_mv | 10.1016/S0014-5793(02)02639-X |
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Trypanosoma brucei brucei TIM were characterized. The folding and stability of the mutants are impaired compared to the wild-type enzyme. This salt bridge is part of a hydrogen bonding network which tethers the C-terminal β7α7β8α8 unit to the bulk of the protein. In the variants D227N, D227A, and R191S, this network is preserved, as can be deduced from the structure of the R191S variant. In the R191A variant, the side chain at position 191 cannot contribute to this network. Also the catalytic power of this variant is most affected.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/S0014-5793(02)02639-X</identifier><identifier>PMID: 11997014</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>Animals ; Arginine - genetics ; Arginine - physiology ; Aspartic Acid - genetics ; Aspartic Acid - physiology ; Binding Sites ; Catalysis ; Conserved Sequence ; DHAP, dihydroxyacetone phosphate ; Enzyme Stability ; Folding ; GAP, glyceraldehyde-3-phosphate ; GuHCl, guanidinium hydrochloride ; Hydrogen Bonding ; Kinetics ; Models, Chemical ; Models, Molecular ; Mutation ; PGA, 2-phosphoglycolate ; Protein Folding ; Salt bridge ; Salts - chemistry ; Stability ; TIM, triosephosphate isomerase ; Triose-Phosphate Isomerase - chemistry ; Triose-Phosphate Isomerase - genetics ; Triose-Phosphate Isomerase - metabolism ; Triosephosphate isomerase ; Trypanosoma brucei brucei - enzymology</subject><ispartof>FEBS letters, 2002-05, Vol.518 (1), p.39-42</ispartof><rights>2002 Federation of European Biochemical Societies</rights><rights>FEBS Letters 518 (2002) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c473X-67e0c242141f5b876c75321dd3edd04cfa9d775cebd064f3f2503975c2db7ed43</citedby><cites>FETCH-LOGICAL-c473X-67e0c242141f5b876c75321dd3edd04cfa9d775cebd064f3f2503975c2db7ed43</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S001457930202639X$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,3549,27924,27925,45780</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11997014$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kursula, Inari</creatorcontrib><creatorcontrib>Partanen, Sanna</creatorcontrib><creatorcontrib>Lambeir, Anne-Marie</creatorcontrib><creatorcontrib>Wierenga, Rik K.</creatorcontrib><title>The importance of the conserved Arg191–Asp227 salt bridge of triosephosphate isomerase for folding, stability, and catalysis</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>Triosephosphate isomerase (TIM) has a conserved salt bridge 20 Å away from both the active site and the dimer interface. In this study, four salt bridge mutants of
Trypanosoma brucei brucei TIM were characterized. The folding and stability of the mutants are impaired compared to the wild-type enzyme. This salt bridge is part of a hydrogen bonding network which tethers the C-terminal β7α7β8α8 unit to the bulk of the protein. In the variants D227N, D227A, and R191S, this network is preserved, as can be deduced from the structure of the R191S variant. In the R191A variant, the side chain at position 191 cannot contribute to this network. Also the catalytic power of this variant is most affected.</description><subject>Animals</subject><subject>Arginine - genetics</subject><subject>Arginine - physiology</subject><subject>Aspartic Acid - genetics</subject><subject>Aspartic Acid - physiology</subject><subject>Binding Sites</subject><subject>Catalysis</subject><subject>Conserved Sequence</subject><subject>DHAP, dihydroxyacetone phosphate</subject><subject>Enzyme Stability</subject><subject>Folding</subject><subject>GAP, glyceraldehyde-3-phosphate</subject><subject>GuHCl, guanidinium hydrochloride</subject><subject>Hydrogen Bonding</subject><subject>Kinetics</subject><subject>Models, Chemical</subject><subject>Models, Molecular</subject><subject>Mutation</subject><subject>PGA, 2-phosphoglycolate</subject><subject>Protein Folding</subject><subject>Salt bridge</subject><subject>Salts - chemistry</subject><subject>Stability</subject><subject>TIM, triosephosphate isomerase</subject><subject>Triose-Phosphate Isomerase - chemistry</subject><subject>Triose-Phosphate Isomerase - genetics</subject><subject>Triose-Phosphate Isomerase - metabolism</subject><subject>Triosephosphate isomerase</subject><subject>Trypanosoma brucei brucei - enzymology</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><recordid>eNqNkc1u1DAUhS1ERaeFRwB5hajUgH-SeLKqhqp_UiUWFGl2lmPfzBglcfDNFM0G8Q68IU-CZzKCZVlYls_97rlXx4S85uw9Z7z88JkxnmeFquQ7Js6YKGWVLZ-RGZ8rmcm8nD8ns7_IMTlB_MrSe86rF-SY86pSqTgjPx7WQH03hDia3gINDR2TYkOPEB_B0UVc8Yr__vlrgYMQiqJpR1pH71YTHH1AGNYBh7UZkxWGDqJBoE2I6bTO96tziqOpfevH7Tk1vaPWjKbdoseX5KgxLcKrw31KvlxfPVzeZvefbu4uF_eZzZVcZqUCZkUueM6bop6r0qpCCu6cBOdYbhtTOaUKC7VjZd7IRhRMVkkQrlbgcnlK3k6-QwzfNoCj7jxaaFvTQ9igVrwsWV4VCSwm0MaAGKHRQ_SdiVvNmd4Fr_fB612qmgm9D14vU9-bw4BN3YH713VIOgG3E_Ddt7D9P1d9ffVR7Cu7AhN7eTfrYrKClNijh6jReki_53wEO2oX_BPb_gGmq6kr</recordid><startdate>20020508</startdate><enddate>20020508</enddate><creator>Kursula, Inari</creator><creator>Partanen, Sanna</creator><creator>Lambeir, Anne-Marie</creator><creator>Wierenga, Rik K.</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20020508</creationdate><title>The importance of the conserved Arg191–Asp227 salt bridge of triosephosphate isomerase for folding, stability, and catalysis</title><author>Kursula, Inari ; Partanen, Sanna ; Lambeir, Anne-Marie ; Wierenga, Rik K.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c473X-67e0c242141f5b876c75321dd3edd04cfa9d775cebd064f3f2503975c2db7ed43</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Animals</topic><topic>Arginine - genetics</topic><topic>Arginine - physiology</topic><topic>Aspartic Acid - genetics</topic><topic>Aspartic Acid - physiology</topic><topic>Binding Sites</topic><topic>Catalysis</topic><topic>Conserved Sequence</topic><topic>DHAP, dihydroxyacetone phosphate</topic><topic>Enzyme Stability</topic><topic>Folding</topic><topic>GAP, glyceraldehyde-3-phosphate</topic><topic>GuHCl, guanidinium hydrochloride</topic><topic>Hydrogen Bonding</topic><topic>Kinetics</topic><topic>Models, Chemical</topic><topic>Models, Molecular</topic><topic>Mutation</topic><topic>PGA, 2-phosphoglycolate</topic><topic>Protein Folding</topic><topic>Salt bridge</topic><topic>Salts - chemistry</topic><topic>Stability</topic><topic>TIM, triosephosphate isomerase</topic><topic>Triose-Phosphate Isomerase - chemistry</topic><topic>Triose-Phosphate Isomerase - genetics</topic><topic>Triose-Phosphate Isomerase - metabolism</topic><topic>Triosephosphate isomerase</topic><topic>Trypanosoma brucei brucei - enzymology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kursula, Inari</creatorcontrib><creatorcontrib>Partanen, Sanna</creatorcontrib><creatorcontrib>Lambeir, Anne-Marie</creatorcontrib><creatorcontrib>Wierenga, Rik K.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kursula, Inari</au><au>Partanen, Sanna</au><au>Lambeir, Anne-Marie</au><au>Wierenga, Rik K.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The importance of the conserved Arg191–Asp227 salt bridge of triosephosphate isomerase for folding, stability, and catalysis</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>2002-05-08</date><risdate>2002</risdate><volume>518</volume><issue>1</issue><spage>39</spage><epage>42</epage><pages>39-42</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>Triosephosphate isomerase (TIM) has a conserved salt bridge 20 Å away from both the active site and the dimer interface. In this study, four salt bridge mutants of
Trypanosoma brucei brucei TIM were characterized. The folding and stability of the mutants are impaired compared to the wild-type enzyme. This salt bridge is part of a hydrogen bonding network which tethers the C-terminal β7α7β8α8 unit to the bulk of the protein. In the variants D227N, D227A, and R191S, this network is preserved, as can be deduced from the structure of the R191S variant. In the R191A variant, the side chain at position 191 cannot contribute to this network. Also the catalytic power of this variant is most affected.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>11997014</pmid><doi>10.1016/S0014-5793(02)02639-X</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Animals Arginine - genetics Arginine - physiology Aspartic Acid - genetics Aspartic Acid - physiology Binding Sites Catalysis Conserved Sequence DHAP, dihydroxyacetone phosphate Enzyme Stability Folding GAP, glyceraldehyde-3-phosphate GuHCl, guanidinium hydrochloride Hydrogen Bonding Kinetics Models, Chemical Models, Molecular Mutation PGA, 2-phosphoglycolate Protein Folding Salt bridge Salts - chemistry Stability TIM, triosephosphate isomerase Triose-Phosphate Isomerase - chemistry Triose-Phosphate Isomerase - genetics Triose-Phosphate Isomerase - metabolism Triosephosphate isomerase Trypanosoma brucei brucei - enzymology |
title | The importance of the conserved Arg191–Asp227 salt bridge of triosephosphate isomerase for folding, stability, and catalysis |
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