Crystallographic binding studies with triosephosphate isomerases: Conformational changes induced by substrate and substrate-analogues
TIM catalyses the interconversion of a triosephosphate aldehyde into a triosephosphate ketone. This is a simple chemical reaction in which only protons are transferred, The crystallographic studies of TIM from chicken, yeast and trypanosome complexed with substrate and substrate analogues are discus...
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| Veröffentlicht in: | FEBS Letters 1992-07, Vol.307 (1), p.34-39 |
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| creator | Wierenga, R.K. Borcher, T.V. Noble, M.E.M. |
| description | TIM catalyses the interconversion of a triosephosphate aldehyde into a triosephosphate ketone. This is a simple chemical reaction in which only protons are transferred, The crystallographic studies of TIM from chicken, yeast and trypanosome complexed with substrate and substrate analogues are discussed. The substrate binds in a deep pocket. On substrate binding, large conformational changes are induced in three loops. As a result of these conformational changes in the liganded Structure, the active site pocket is sealed off from bulk solvent and the sidechain of the catalytic glutamate becomes optimally positioned for catalysis. |
| doi_str_mv | 10.1016/0014-5793(92)80897-P |
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This is a simple chemical reaction in which only protons are transferred, The crystallographic studies of TIM from chicken, yeast and trypanosome complexed with substrate and substrate analogues are discussed. The substrate binds in a deep pocket. On substrate binding, large conformational changes are induced in three loops. As a result of these conformational changes in the liganded Structure, the active site pocket is sealed off from bulk solvent and the sidechain of the catalytic glutamate becomes optimally positioned for catalysis.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/0014-5793(92)80897-P</identifier><identifier>PMID: 1639191</identifier><identifier>CODEN: FEBLAL</identifier><language>eng</language><publisher>Amsterdam: Elsevier B.V</publisher><subject>2-phosphoglycollate ; 2PG ; Analytical, structural and metabolic biochemistry ; Biological and medical sciences ; Catalysis ; chickens ; conformation ; Conformational change ; Crystallographic binding study ; d-glyceraldehyde-3-phosphate ; DHAP ; dihydroxyacetone phosphate ; Dimer ; Enzymes and enzyme inhibitors ; Fundamental and applied biological sciences. Psychology ; G3P ; GAP ; glycerol-3-phosphate ; interaction ; Isomerases ; Ligands ; PGH ; phosphoglycolohydroxamate ; Protein Conformation ; reviews ; RMS ; root mean square ; Saccharomyces cerevisiae ; Substrate Specificity ; substrates ; TIM ; triose-phosphate isomerase ; Triose-Phosphate Isomerase - chemistry ; Triose-Phosphate Isomerase - metabolism ; Triosephosphate isomerase ; triosephosphate isomerase (E.C, 5.3.1.1.) ; X-ray crystallography ; X-Ray Diffraction</subject><ispartof>FEBS Letters, 1992-07, Vol.307 (1), p.34-39</ispartof><rights>1992</rights><rights>FEBS Letters 307 (1992) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><rights>1992 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c480P-bb9e5d7b8a4ab42a62ae0a2a4a36aedc2710fe48d11912e415f07144b62b05213</citedby><cites>FETCH-LOGICAL-c480P-bb9e5d7b8a4ab42a62ae0a2a4a36aedc2710fe48d11912e415f07144b62b05213</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/001457939280897P$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>313,314,776,780,788,3537,27899,27901,27902,65534</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=5397158$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1639191$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wierenga, R.K.</creatorcontrib><creatorcontrib>Borcher, T.V.</creatorcontrib><creatorcontrib>Noble, M.E.M.</creatorcontrib><title>Crystallographic binding studies with triosephosphate isomerases: Conformational changes induced by substrate and substrate-analogues</title><title>FEBS Letters</title><addtitle>FEBS Lett</addtitle><description>TIM catalyses the interconversion of a triosephosphate aldehyde into a triosephosphate ketone. This is a simple chemical reaction in which only protons are transferred, The crystallographic studies of TIM from chicken, yeast and trypanosome complexed with substrate and substrate analogues are discussed. The substrate binds in a deep pocket. On substrate binding, large conformational changes are induced in three loops. As a result of these conformational changes in the liganded Structure, the active site pocket is sealed off from bulk solvent and the sidechain of the catalytic glutamate becomes optimally positioned for catalysis.</description><subject>2-phosphoglycollate</subject><subject>2PG</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Biological and medical sciences</subject><subject>Catalysis</subject><subject>chickens</subject><subject>conformation</subject><subject>Conformational change</subject><subject>Crystallographic binding study</subject><subject>d-glyceraldehyde-3-phosphate</subject><subject>DHAP</subject><subject>dihydroxyacetone phosphate</subject><subject>Dimer</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>G3P</subject><subject>GAP</subject><subject>glycerol-3-phosphate</subject><subject>interaction</subject><subject>Isomerases</subject><subject>Ligands</subject><subject>PGH</subject><subject>phosphoglycolohydroxamate</subject><subject>Protein Conformation</subject><subject>reviews</subject><subject>RMS</subject><subject>root mean square</subject><subject>Saccharomyces cerevisiae</subject><subject>Substrate Specificity</subject><subject>substrates</subject><subject>TIM</subject><subject>triose-phosphate isomerase</subject><subject>Triose-Phosphate Isomerase - chemistry</subject><subject>Triose-Phosphate Isomerase - metabolism</subject><subject>Triosephosphate isomerase</subject><subject>triosephosphate isomerase (E.C, 5.3.1.1.)</subject><subject>X-ray crystallography</subject><subject>X-Ray Diffraction</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNUc1u1DAQjhCoLIU3ACkHhOAQsB3nxz0g0VUXkCqxBzhbE2eyMUri4Emo9gH63jjNqr0BJ2vm-5kZf1H0krP3nPH8A2NcJlmh0rdKvCtZqYpk_yja8LJIk1Tm5eNoc095Gj0j-slCXXJ1Fp3xPFVc8U10u_VHmqDr3MHD2FoTV3ao7XCIaZprixTf2KmNJ28d4dg6GluYMLbkevRASBfx1g2N8z1M1g3QxaaF4RB0wWY2WMfVMaa5oskvOhjqhyqBwHeHGel59KSBjvDF6T2Pfuyuvm-_JNffPn_dfrpOjCzZPqkqhVldVCVIqKSAXAAyEKFKc8DaiIKzBmVZ83CbQMmzhhVcyioXFcsET8-jN6vv6N2vMHfSvSWDXQcDupl0kTJVsrz8J5HnUmRC5oEoV6Lxjshjo0dve_BHzZleYtJLBnrJQCuh72LS-yB7dfKfqx7rB9GaS8Bfn3AgA13jYTCW7mlZqgqeLWvuVtqN7fD4X6P17upSLMDSV-Kuu-zzcTXC8Pu_LXpNxuIQ8rMezaRrZ_9-0B9j4sXH</recordid><startdate>19920727</startdate><enddate>19920727</enddate><creator>Wierenga, R.K.</creator><creator>Borcher, T.V.</creator><creator>Noble, M.E.M.</creator><general>Elsevier B.V</general><general>Elsevier</general><scope>6I.</scope><scope>AAFTH</scope><scope>IQODW</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>7QL</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>19920727</creationdate><title>Crystallographic binding studies with triosephosphate isomerases: Conformational changes induced by substrate and substrate-analogues</title><author>Wierenga, R.K. ; Borcher, T.V. ; Noble, M.E.M.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c480P-bb9e5d7b8a4ab42a62ae0a2a4a36aedc2710fe48d11912e415f07144b62b05213</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>2-phosphoglycollate</topic><topic>2PG</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Biological and medical sciences</topic><topic>Catalysis</topic><topic>chickens</topic><topic>conformation</topic><topic>Conformational change</topic><topic>Crystallographic binding study</topic><topic>d-glyceraldehyde-3-phosphate</topic><topic>DHAP</topic><topic>dihydroxyacetone phosphate</topic><topic>Dimer</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>G3P</topic><topic>GAP</topic><topic>glycerol-3-phosphate</topic><topic>interaction</topic><topic>Isomerases</topic><topic>Ligands</topic><topic>PGH</topic><topic>phosphoglycolohydroxamate</topic><topic>Protein Conformation</topic><topic>reviews</topic><topic>RMS</topic><topic>root mean square</topic><topic>Saccharomyces cerevisiae</topic><topic>Substrate Specificity</topic><topic>substrates</topic><topic>TIM</topic><topic>triose-phosphate isomerase</topic><topic>Triose-Phosphate Isomerase - chemistry</topic><topic>Triose-Phosphate Isomerase - metabolism</topic><topic>Triosephosphate isomerase</topic><topic>triosephosphate isomerase (E.C, 5.3.1.1.)</topic><topic>X-ray crystallography</topic><topic>X-Ray Diffraction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wierenga, R.K.</creatorcontrib><creatorcontrib>Borcher, T.V.</creatorcontrib><creatorcontrib>Noble, M.E.M.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>FEBS Letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wierenga, R.K.</au><au>Borcher, T.V.</au><au>Noble, M.E.M.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Crystallographic binding studies with triosephosphate isomerases: Conformational changes induced by substrate and substrate-analogues</atitle><jtitle>FEBS Letters</jtitle><addtitle>FEBS Lett</addtitle><date>1992-07-27</date><risdate>1992</risdate><volume>307</volume><issue>1</issue><spage>34</spage><epage>39</epage><pages>34-39</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><coden>FEBLAL</coden><abstract>TIM catalyses the interconversion of a triosephosphate aldehyde into a triosephosphate ketone. This is a simple chemical reaction in which only protons are transferred, The crystallographic studies of TIM from chicken, yeast and trypanosome complexed with substrate and substrate analogues are discussed. The substrate binds in a deep pocket. On substrate binding, large conformational changes are induced in three loops. As a result of these conformational changes in the liganded Structure, the active site pocket is sealed off from bulk solvent and the sidechain of the catalytic glutamate becomes optimally positioned for catalysis.</abstract><cop>Amsterdam</cop><pub>Elsevier B.V</pub><pmid>1639191</pmid><doi>10.1016/0014-5793(92)80897-P</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Elsevier ScienceDirect Journals Complete; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | 2-phosphoglycollate 2PG Analytical, structural and metabolic biochemistry Biological and medical sciences Catalysis chickens conformation Conformational change Crystallographic binding study d-glyceraldehyde-3-phosphate DHAP dihydroxyacetone phosphate Dimer Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology G3P GAP glycerol-3-phosphate interaction Isomerases Ligands PGH phosphoglycolohydroxamate Protein Conformation reviews RMS root mean square Saccharomyces cerevisiae Substrate Specificity substrates TIM triose-phosphate isomerase Triose-Phosphate Isomerase - chemistry Triose-Phosphate Isomerase - metabolism Triosephosphate isomerase triosephosphate isomerase (E.C, 5.3.1.1.) X-ray crystallography X-Ray Diffraction |
| title | Crystallographic binding studies with triosephosphate isomerases: Conformational changes induced by substrate and substrate-analogues |
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