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A possible nucleotide-binding domain in the tertiary fold of phosphoribosyltransferases
Comparison of the primary structures of three phosphoribosyltransferases (human hypoxanthine-guanine, Salmonella typhimurium ATP, and Escherichia coli glutamine) showed no significant amino acid sequence homology except for a 35-residue span in hypoxanthine-guanine and glutamine phosphoribosyltransf...
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Published in: | The Journal of biological chemistry 1983-05, Vol.258 (10), p.6450-6457 |
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creator | Argos, P Hanei, M Wilson, J M Kelley, W N |
description | Comparison of the primary structures of three phosphoribosyltransferases (human hypoxanthine-guanine, Salmonella typhimurium ATP, and Escherichia coli glutamine) showed no significant amino acid sequence homology except for a 35-residue span in hypoxanthine-guanine and glutamine phosphoribosyltransferases. However, comparison of smoothed plots of amino acid physical characteristics thought to control protein folding with amino acid sequence number resulted in a substantial correlation for a 120-residue stretch in each of the phosphoribosyltransferases. A secondary structure prediction analysis of the regions indicated a dinucleotide-binding fold with its characteristic beta alpha beta secondary structural pattern. Furthermore, the physical parametric correlation analysis suggested a common catalytic domain fold for hypoxanthine-guanine and glutamine phosphoribosyltransferases which was consistent with the register of the sequence homology. A possible binding mode of the phosphoribosyltransferase substrates is discussed. The physical parametric approach to protein sequence comparison may be generally applicable for distantly related proteins which maintain similar structural folds without any apparent sequence homology. |
doi_str_mv | 10.1016/S0021-9258(18)32431-1 |
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However, comparison of smoothed plots of amino acid physical characteristics thought to control protein folding with amino acid sequence number resulted in a substantial correlation for a 120-residue stretch in each of the phosphoribosyltransferases. A secondary structure prediction analysis of the regions indicated a dinucleotide-binding fold with its characteristic beta alpha beta secondary structural pattern. Furthermore, the physical parametric correlation analysis suggested a common catalytic domain fold for hypoxanthine-guanine and glutamine phosphoribosyltransferases which was consistent with the register of the sequence homology. A possible binding mode of the phosphoribosyltransferase substrates is discussed. 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The physical parametric approach to protein sequence comparison may be generally applicable for distantly related proteins which maintain similar structural folds without any apparent sequence homology.</description><subject>Amidophosphoribosyltransferase - metabolism</subject><subject>Amino Acid Sequence</subject><subject>ATP Phosphoribosyltransferase - metabolism</subject><subject>Binding Sites</subject><subject>Escherichia coli - enzymology</subject><subject>Humans</subject><subject>Hypoxanthine Phosphoribosyltransferase - metabolism</subject><subject>L-Lactate Dehydrogenase</subject><subject>Nucleotides - metabolism</subject><subject>Pentosyltransferases - metabolism</subject><subject>Protein Conformation</subject><subject>Salmonella typhimurium - enzymology</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1983</creationdate><recordtype>article</recordtype><recordid>eNqFkMtKxDAUhoMoOl4eQSgIootq0qRtupJBvMGACxXdhVxOp5G2GZNW8e3NXJitISGL8_0nOR9CpwRfEUyK6xeMM5JWWc4vCL-kGaMkJTtoQjCnKc3Jxy6abJEDdBjCJ46LVWQf7ReUUVqWE_Q-TRYuBKtaSPpRt-AGayBVtje2nyfGddL2SdxDA8kAfrDS_ya1a03i6mTRuBCPt8qF33bwsg81eBkgHKO9WrYBTjb3EXq7v3u9fUxnzw9Pt9NZqhnNh5TVBQVJCTasMrTKaIZxJRVmuc4KXiuDaZkZ4FBSqmWsFBFUyhDCSgMxeYTO130X3n2NEAbR2aChbWUPbgyCY8Y5rlgE8zWofZzXQy0W3nZxGEGwWAoVK6FiaUsQLlZCBYm5080Do-rAbFMbg7F-tq43dt78WA9CWacb6MSqERYFy3GkbtYURBffFrwI2kKvwcSEHoRx9p9__AFXSZJV</recordid><startdate>19830525</startdate><enddate>19830525</enddate><creator>Argos, P</creator><creator>Hanei, M</creator><creator>Wilson, J M</creator><creator>Kelley, W N</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</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>19830525</creationdate><title>A possible nucleotide-binding domain in the tertiary fold of phosphoribosyltransferases</title><author>Argos, P ; Hanei, M ; Wilson, J M ; Kelley, W N</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c435t-4f63ea310d49d39232009ab045c268fbd0372de8e733ca9ab6d49bbd1147deea3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1983</creationdate><topic>Amidophosphoribosyltransferase - metabolism</topic><topic>Amino Acid Sequence</topic><topic>ATP Phosphoribosyltransferase - metabolism</topic><topic>Binding Sites</topic><topic>Escherichia coli - enzymology</topic><topic>Humans</topic><topic>Hypoxanthine Phosphoribosyltransferase - metabolism</topic><topic>L-Lactate Dehydrogenase</topic><topic>Nucleotides - metabolism</topic><topic>Pentosyltransferases - metabolism</topic><topic>Protein Conformation</topic><topic>Salmonella typhimurium - enzymology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Argos, P</creatorcontrib><creatorcontrib>Hanei, M</creatorcontrib><creatorcontrib>Wilson, J M</creatorcontrib><creatorcontrib>Kelley, W N</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>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Argos, P</au><au>Hanei, M</au><au>Wilson, J M</au><au>Kelley, W N</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A possible nucleotide-binding domain in the tertiary fold of phosphoribosyltransferases</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1983-05-25</date><risdate>1983</risdate><volume>258</volume><issue>10</issue><spage>6450</spage><epage>6457</epage><pages>6450-6457</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>Comparison of the primary structures of three phosphoribosyltransferases (human hypoxanthine-guanine, Salmonella typhimurium ATP, and Escherichia coli glutamine) showed no significant amino acid sequence homology except for a 35-residue span in hypoxanthine-guanine and glutamine phosphoribosyltransferases. However, comparison of smoothed plots of amino acid physical characteristics thought to control protein folding with amino acid sequence number resulted in a substantial correlation for a 120-residue stretch in each of the phosphoribosyltransferases. A secondary structure prediction analysis of the regions indicated a dinucleotide-binding fold with its characteristic beta alpha beta secondary structural pattern. Furthermore, the physical parametric correlation analysis suggested a common catalytic domain fold for hypoxanthine-guanine and glutamine phosphoribosyltransferases which was consistent with the register of the sequence homology. A possible binding mode of the phosphoribosyltransferase substrates is discussed. 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subjects | Amidophosphoribosyltransferase - metabolism Amino Acid Sequence ATP Phosphoribosyltransferase - metabolism Binding Sites Escherichia coli - enzymology Humans Hypoxanthine Phosphoribosyltransferase - metabolism L-Lactate Dehydrogenase Nucleotides - metabolism Pentosyltransferases - metabolism Protein Conformation Salmonella typhimurium - enzymology |
title | A possible nucleotide-binding domain in the tertiary fold of phosphoribosyltransferases |
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