Anion binding at the active site of trypanosomal triosephosphate isomerase: monohydrogen phosphate does not mimic sulphate
The three-dimensional structure of triosephosphate isomerase complexed with the competitive inhibitor HP024- was determined by x-ray crystallography to a resolution of 0.24 nm. A comparison with the native crystal structure, where, SO24- is bound, revealed five changes: (a) a 0.10-nm shift of the an...
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| Veröffentlicht in: | European journal of biochemistry 1991-05, Vol.198 (1), p.53-57 |
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| container_title | European journal of biochemistry |
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| creator | Verlinde, C.L.M.J. (University of Groningen, Groningen, The Netherlands) Noble, M.E.M Kalk, K.H Groendijk, H Wierenga, R.K Hol, W.G.J |
| description | The three-dimensional structure of triosephosphate isomerase complexed with the competitive inhibitor HP024- was determined by x-ray crystallography to a resolution of 0.24 nm. A comparison with the native crystal structure, where, SO24- is bound, revealed five changes: (a) a 0.10-nm shift of the anion-binding site; (b) a further closing of the flexible loop of the enzyme; (c) a 'swinging in' of the side chain of the catalytic Glu, that is X1 changes from (+) to (-) synclinal; (d) an altered water structure; (e) a disappearance of the conformational heterogeneity at the C-terminus of strand beta 7. Some of these changes may be related to the different hydrogen-bond pattern about the two different anions. However, the distance of 0.10 nm between the sulphur and phosphorus positions is unexpected and remains intriguing |
| doi_str_mv | 10.1111/j.1432-1033.1991.tb15985.x |
| format | Article |
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(University of Groningen, Groningen, The Netherlands) ; Noble, M.E.M ; Kalk, K.H ; Groendijk, H ; Wierenga, R.K ; Hol, W.G.J</creator><creatorcontrib>Verlinde, C.L.M.J. (University of Groningen, Groningen, The Netherlands) ; Noble, M.E.M ; Kalk, K.H ; Groendijk, H ; Wierenga, R.K ; Hol, W.G.J</creatorcontrib><description>The three-dimensional structure of triosephosphate isomerase complexed with the competitive inhibitor HP024- was determined by x-ray crystallography to a resolution of 0.24 nm. A comparison with the native crystal structure, where, SO24- is bound, revealed five changes: (a) a 0.10-nm shift of the anion-binding site; (b) a further closing of the flexible loop of the enzyme; (c) a 'swinging in' of the side chain of the catalytic Glu, that is X1 changes from (+) to (-) synclinal; (d) an altered water structure; (e) a disappearance of the conformational heterogeneity at the C-terminus of strand beta 7. Some of these changes may be related to the different hydrogen-bond pattern about the two different anions. However, the distance of 0.10 nm between the sulphur and phosphorus positions is unexpected and remains intriguing</description><identifier>ISSN: 0014-2956</identifier><identifier>EISSN: 1432-1033</identifier><identifier>DOI: 10.1111/j.1432-1033.1991.tb15985.x</identifier><identifier>PMID: 2040290</identifier><identifier>CODEN: EJBCAI</identifier><language>eng</language><publisher>Oxford: Blackwell</publisher><subject>Analytical, structural and metabolic biochemistry ; Animals ; ANION ; ANIONES ; Anions - metabolism ; AZUFRE ; Binding Sites ; Biological and medical sciences ; CHIMIE ; Enzymes and enzyme inhibitors ; FOSFATOS ; FOSFORO ; Fundamental and applied biological sciences. Psychology ; ISOMERASAS ; ISOMERASE ; Isomerases ; Molecular Structure ; MONOSACARIDOS ; MONOSACCHARIDE ; ORGANITE CELLULAIRE ; Organophosphorus Compounds - metabolism ; ORGANULOS CITOPLASMATICOS ; PHOSPHATE ; PHOSPHORE ; QUIMICA ; SOUFRE ; Sulfuric Acids - metabolism ; Triose-Phosphate Isomerase - metabolism ; TRYPANOSOMA BRUCEI ; Trypanosoma brucei brucei - enzymology ; X-Ray Diffraction</subject><ispartof>European journal of biochemistry, 1991-05, Vol.198 (1), p.53-57</ispartof><rights>1993 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c336t-b038eee051d0bed84aec45279bd7e9eecb0642f860296e7ac4158a2887da75dd3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4565353$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2040290$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Verlinde, C.L.M.J. (University of Groningen, Groningen, The Netherlands)</creatorcontrib><creatorcontrib>Noble, M.E.M</creatorcontrib><creatorcontrib>Kalk, K.H</creatorcontrib><creatorcontrib>Groendijk, H</creatorcontrib><creatorcontrib>Wierenga, R.K</creatorcontrib><creatorcontrib>Hol, W.G.J</creatorcontrib><title>Anion binding at the active site of trypanosomal triosephosphate isomerase: monohydrogen phosphate does not mimic sulphate</title><title>European journal of biochemistry</title><addtitle>Eur J Biochem</addtitle><description>The three-dimensional structure of triosephosphate isomerase complexed with the competitive inhibitor HP024- was determined by x-ray crystallography to a resolution of 0.24 nm. A comparison with the native crystal structure, where, SO24- is bound, revealed five changes: (a) a 0.10-nm shift of the anion-binding site; (b) a further closing of the flexible loop of the enzyme; (c) a 'swinging in' of the side chain of the catalytic Glu, that is X1 changes from (+) to (-) synclinal; (d) an altered water structure; (e) a disappearance of the conformational heterogeneity at the C-terminus of strand beta 7. Some of these changes may be related to the different hydrogen-bond pattern about the two different anions. However, the distance of 0.10 nm between the sulphur and phosphorus positions is unexpected and remains intriguing</description><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>ANION</subject><subject>ANIONES</subject><subject>Anions - metabolism</subject><subject>AZUFRE</subject><subject>Binding Sites</subject><subject>Biological and medical sciences</subject><subject>CHIMIE</subject><subject>Enzymes and enzyme inhibitors</subject><subject>FOSFATOS</subject><subject>FOSFORO</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>ISOMERASAS</subject><subject>ISOMERASE</subject><subject>Isomerases</subject><subject>Molecular Structure</subject><subject>MONOSACARIDOS</subject><subject>MONOSACCHARIDE</subject><subject>ORGANITE CELLULAIRE</subject><subject>Organophosphorus Compounds - metabolism</subject><subject>ORGANULOS CITOPLASMATICOS</subject><subject>PHOSPHATE</subject><subject>PHOSPHORE</subject><subject>QUIMICA</subject><subject>SOUFRE</subject><subject>Sulfuric Acids - metabolism</subject><subject>Triose-Phosphate Isomerase - metabolism</subject><subject>TRYPANOSOMA BRUCEI</subject><subject>Trypanosoma brucei brucei - enzymology</subject><subject>X-Ray Diffraction</subject><issn>0014-2956</issn><issn>1432-1033</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1991</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUFv1DAQhS0EKkvhDyAhWQj1lmAnsWP3VlUUkCpxgJ4tx57sepXYwc5WXX49Tjdajvhied43b8Z6CH2kpKT5fN6XtKmrgpK6LqmUtJw7yqRg5dMLtDlLL9GGENoUlWT8NXqT0p4QwiVvL9BFRRpSSbJBf268Cx53zlvnt1jPeN4B1mZ2j4CTmwGHHs_xOGkfUhj1kB8uJJh2IU07nXWXyxB1gms8Bh92RxvDFjz-R9gACfsw49GNzuB0GJ7rb9GrXg8J3q33JXq4-_Lr9ltx_-Pr99ub-8LUNZ-LjtQCAAijlnRgRaPBNKxqZWdbkACmI7ypesHzhzi02jSUCV0J0VrdMmvrS3R18p1i-H2ANKvRJQPDoD2EQ1KCMMGlqP8LUi4E5WwBr0-giSGlCL2aoht1PCpK1JKQ2qslBrXEoJaE1JqQesrNH9Yph24Ee25dI8n6p1XXyeihj9obl85Yw_IGzzu8P2G9DkpvY0YefkqaHbLHX50JpgU</recordid><startdate>19910523</startdate><enddate>19910523</enddate><creator>Verlinde, C.L.M.J. (University of Groningen, Groningen, The Netherlands)</creator><creator>Noble, M.E.M</creator><creator>Kalk, K.H</creator><creator>Groendijk, H</creator><creator>Wierenga, R.K</creator><creator>Hol, W.G.J</creator><general>Blackwell</general><scope>FBQ</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>M7N</scope><scope>7X8</scope></search><sort><creationdate>19910523</creationdate><title>Anion binding at the active site of trypanosomal triosephosphate isomerase: monohydrogen phosphate does not mimic sulphate</title><author>Verlinde, C.L.M.J. (University of Groningen, Groningen, The Netherlands) ; Noble, M.E.M ; Kalk, K.H ; Groendijk, H ; Wierenga, R.K ; Hol, W.G.J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c336t-b038eee051d0bed84aec45279bd7e9eecb0642f860296e7ac4158a2887da75dd3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1991</creationdate><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>ANION</topic><topic>ANIONES</topic><topic>Anions - metabolism</topic><topic>AZUFRE</topic><topic>Binding Sites</topic><topic>Biological and medical sciences</topic><topic>CHIMIE</topic><topic>Enzymes and enzyme inhibitors</topic><topic>FOSFATOS</topic><topic>FOSFORO</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>ISOMERASAS</topic><topic>ISOMERASE</topic><topic>Isomerases</topic><topic>Molecular Structure</topic><topic>MONOSACARIDOS</topic><topic>MONOSACCHARIDE</topic><topic>ORGANITE CELLULAIRE</topic><topic>Organophosphorus Compounds - metabolism</topic><topic>ORGANULOS CITOPLASMATICOS</topic><topic>PHOSPHATE</topic><topic>PHOSPHORE</topic><topic>QUIMICA</topic><topic>SOUFRE</topic><topic>Sulfuric Acids - metabolism</topic><topic>Triose-Phosphate Isomerase - metabolism</topic><topic>TRYPANOSOMA BRUCEI</topic><topic>Trypanosoma brucei brucei - enzymology</topic><topic>X-Ray Diffraction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Verlinde, C.L.M.J. (University of Groningen, Groningen, The Netherlands)</creatorcontrib><creatorcontrib>Noble, M.E.M</creatorcontrib><creatorcontrib>Kalk, K.H</creatorcontrib><creatorcontrib>Groendijk, H</creatorcontrib><creatorcontrib>Wierenga, R.K</creatorcontrib><creatorcontrib>Hol, W.G.J</creatorcontrib><collection>AGRIS</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>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>MEDLINE - Academic</collection><jtitle>European journal of biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Verlinde, C.L.M.J. (University of Groningen, Groningen, The Netherlands)</au><au>Noble, M.E.M</au><au>Kalk, K.H</au><au>Groendijk, H</au><au>Wierenga, R.K</au><au>Hol, W.G.J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Anion binding at the active site of trypanosomal triosephosphate isomerase: monohydrogen phosphate does not mimic sulphate</atitle><jtitle>European journal of biochemistry</jtitle><addtitle>Eur J Biochem</addtitle><date>1991-05-23</date><risdate>1991</risdate><volume>198</volume><issue>1</issue><spage>53</spage><epage>57</epage><pages>53-57</pages><issn>0014-2956</issn><eissn>1432-1033</eissn><coden>EJBCAI</coden><abstract>The three-dimensional structure of triosephosphate isomerase complexed with the competitive inhibitor HP024- was determined by x-ray crystallography to a resolution of 0.24 nm. A comparison with the native crystal structure, where, SO24- is bound, revealed five changes: (a) a 0.10-nm shift of the anion-binding site; (b) a further closing of the flexible loop of the enzyme; (c) a 'swinging in' of the side chain of the catalytic Glu, that is X1 changes from (+) to (-) synclinal; (d) an altered water structure; (e) a disappearance of the conformational heterogeneity at the C-terminus of strand beta 7. Some of these changes may be related to the different hydrogen-bond pattern about the two different anions. However, the distance of 0.10 nm between the sulphur and phosphorus positions is unexpected and remains intriguing</abstract><cop>Oxford</cop><pub>Blackwell</pub><pmid>2040290</pmid><doi>10.1111/j.1432-1033.1991.tb15985.x</doi><tpages>5</tpages></addata></record> |
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| subjects | Analytical, structural and metabolic biochemistry Animals ANION ANIONES Anions - metabolism AZUFRE Binding Sites Biological and medical sciences CHIMIE Enzymes and enzyme inhibitors FOSFATOS FOSFORO Fundamental and applied biological sciences. Psychology ISOMERASAS ISOMERASE Isomerases Molecular Structure MONOSACARIDOS MONOSACCHARIDE ORGANITE CELLULAIRE Organophosphorus Compounds - metabolism ORGANULOS CITOPLASMATICOS PHOSPHATE PHOSPHORE QUIMICA SOUFRE Sulfuric Acids - metabolism Triose-Phosphate Isomerase - metabolism TRYPANOSOMA BRUCEI Trypanosoma brucei brucei - enzymology X-Ray Diffraction |
| title | Anion binding at the active site of trypanosomal triosephosphate isomerase: monohydrogen phosphate does not mimic sulphate |
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