Structural determinants for ligand binding and catalysis of triosephosphate isomerase
The crystal structure of leishmania triosephosphate isomerase (TIM) complexed with 2‐(N‐formyl‐N‐hydroxy)‐aminoethyl phosphonate (IPP) highlights the importance of Asn11 for binding and catalysis. IPP is an analogue of the substrate d‐glyceraldehyde‐3‐phosphate, and it is observed to bind with its a...
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| Veröffentlicht in: | European journal of biochemistry 2001-10, Vol.268 (19), p.5189-5196 |
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| container_title | European journal of biochemistry |
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| creator | Kursula, Inari Partanen, Sanna Lambeir, Anne‐Marie Antonov, Dmitry M. Augustyns, Koen Wierenga, Rik K. |
| description | The crystal structure of leishmania triosephosphate isomerase (TIM) complexed with 2‐(N‐formyl‐N‐hydroxy)‐aminoethyl phosphonate (IPP) highlights the importance of Asn11 for binding and catalysis. IPP is an analogue of the substrate d‐glyceraldehyde‐3‐phosphate, and it is observed to bind with its aldehyde oxygen in an oxyanion hole formed by ND2 of Asn11 and NE2 of His95. Comparison of the mode of binding of IPP and the transition state analogue phosphoglycolohydroxamate (PGH) suggests that the Glu167 side chain, as well as the triose part of the substrate, adopt different conformations as the catalysed reaction proceeds. Comparison of the TIM–IPP and the TIM–PGH structures with other liganded and unliganded structures also highlights the conformational flexibility of the ligand and the active site, as well as the conserved mode of ligand binding. |
| doi_str_mv | 10.1046/j.0014-2956.2001.02452.x |
| format | Article |
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triosephosphate isomerase</title><title>European journal of biochemistry</title><addtitle>Eur J Biochem</addtitle><description>The crystal structure of leishmania triosephosphate isomerase (TIM) complexed with 2‐(N‐formyl‐N‐hydroxy)‐aminoethyl phosphonate (IPP) highlights the importance of Asn11 for binding and catalysis. IPP is an analogue of the substrate d‐glyceraldehyde‐3‐phosphate, and it is observed to bind with its aldehyde oxygen in an oxyanion hole formed by ND2 of Asn11 and NE2 of His95. Comparison of the mode of binding of IPP and the transition state analogue phosphoglycolohydroxamate (PGH) suggests that the Glu167 side chain, as well as the triose part of the substrate, adopt different conformations as the catalysed reaction proceeds. Comparison of the TIM–IPP and the TIM–PGH structures with other liganded and unliganded structures also highlights the conformational flexibility of the ligand and the active site, as well as the conserved mode of ligand binding.</description><subject>Aminoethylphosphonic Acid - analogs & derivatives</subject><subject>Aminoethylphosphonic Acid - metabolism</subject><subject>Animals</subject><subject>Asparagine - metabolism</subject><subject>Catalysis</subject><subject>Crystallography, X-Ray</subject><subject>Enzyme Inhibitors - pharmacology</subject><subject>hydroxamate</subject><subject>Leishmania - enzymology</subject><subject>Ligands</subject><subject>Models, Molecular</subject><subject>Organophosphonates</subject><subject>oxyanion hole</subject><subject>Protein Conformation</subject><subject>Substrate Specificity</subject><subject>TIM</subject><subject>transition state analogue</subject><subject>Triose-Phosphate Isomerase - antagonists & inhibitors</subject><subject>Triose-Phosphate Isomerase - chemistry</subject><subject>Triose-Phosphate Isomerase - isolation & purification</subject><subject>Triose-Phosphate Isomerase - metabolism</subject><issn>0014-2956</issn><issn>1432-1033</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkE1OwzAQRi0EglK4AvKKXYLHTpxkgwQVBaRKLAoSO8t1JsVVfoqdCLrjOJyLk5DQCras5hvpfTPSI4QCC4FF8mIVMgZRwLNYhryPIeNRzMP3PTKCSPAAmBD7ZPQLHZFj71eMMZnJ5JAcAcRplgCMyPO8dZ1pO6dLmmOLrrK1rltPi8bR0i51ndOFrXNbL-mQjW51ufHW06agXx-frbONx_VL49cvukVqfVOh0x5PyEGhS4-nuzkmT9Obx8ldMHu4vZ9czQITgeRBwYWRiQQQWRRnOUOdIJPxohCGS16kOtcC037nKeM8gSgDyRKE2EDGcjRiTM63d9euee3Qt6qy3mBZ6hqbzquEQ8riVPZgugWNa7x3WKi1s5V2GwVMDVbVSg3C1CBMDVbVj1X13lfPdj-6RYX5X3GnsQcut8CbLXHz78NqenM9H6L4BvWEh88</recordid><startdate>200110</startdate><enddate>200110</enddate><creator>Kursula, Inari</creator><creator>Partanen, Sanna</creator><creator>Lambeir, Anne‐Marie</creator><creator>Antonov, Dmitry M.</creator><creator>Augustyns, Koen</creator><creator>Wierenga, Rik K.</creator><general>Blackwell Science Ltd</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><scope>7X8</scope></search><sort><creationdate>200110</creationdate><title>Structural determinants for ligand binding and catalysis of
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triosephosphate isomerase</atitle><jtitle>European journal of biochemistry</jtitle><addtitle>Eur J Biochem</addtitle><date>2001-10</date><risdate>2001</risdate><volume>268</volume><issue>19</issue><spage>5189</spage><epage>5196</epage><pages>5189-5196</pages><issn>0014-2956</issn><eissn>1432-1033</eissn><abstract>The crystal structure of leishmania triosephosphate isomerase (TIM) complexed with 2‐(N‐formyl‐N‐hydroxy)‐aminoethyl phosphonate (IPP) highlights the importance of Asn11 for binding and catalysis. IPP is an analogue of the substrate d‐glyceraldehyde‐3‐phosphate, and it is observed to bind with its aldehyde oxygen in an oxyanion hole formed by ND2 of Asn11 and NE2 of His95. Comparison of the mode of binding of IPP and the transition state analogue phosphoglycolohydroxamate (PGH) suggests that the Glu167 side chain, as well as the triose part of the substrate, adopt different conformations as the catalysed reaction proceeds. Comparison of the TIM–IPP and the TIM–PGH structures with other liganded and unliganded structures also highlights the conformational flexibility of the ligand and the active site, as well as the conserved mode of ligand binding.</abstract><cop>Oxford, UK</cop><pub>Blackwell Science Ltd</pub><pmid>11589711</pmid><doi>10.1046/j.0014-2956.2001.02452.x</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | European journal of biochemistry, 2001-10, Vol.268 (19), p.5189-5196 |
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| subjects | Aminoethylphosphonic Acid - analogs & derivatives Aminoethylphosphonic Acid - metabolism Animals Asparagine - metabolism Catalysis Crystallography, X-Ray Enzyme Inhibitors - pharmacology hydroxamate Leishmania - enzymology Ligands Models, Molecular Organophosphonates oxyanion hole Protein Conformation Substrate Specificity TIM transition state analogue Triose-Phosphate Isomerase - antagonists & inhibitors Triose-Phosphate Isomerase - chemistry Triose-Phosphate Isomerase - isolation & purification Triose-Phosphate Isomerase - metabolism |
| title | Structural determinants for ligand binding and catalysis of
triosephosphate isomerase |
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