2iyo
From Proteopedia
(New page: 200px<br /> <applet load="2iyo" size="450" color="white" frame="true" align="right" spinBox="true" caption="2iyo, resolution 2.40Å" /> '''STRUCTURAL CHARACTE...) |
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==About this Structure== | ==About this Structure== | ||
| - | 2IYO is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Lactococcus_lactis Lactococcus lactis]] with 6PG and CAC as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.44 1.1.1.44]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2IYO OCA]]. | + | 2IYO is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Lactococcus_lactis Lactococcus lactis]] with 6PG and CAC as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Phosphogluconate_dehydrogenase_(decarboxylating) Phosphogluconate dehydrogenase (decarboxylating)]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.44 1.1.1.44]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2IYO OCA]]. |
==Reference== | ==Reference== | ||
Crystal structures of a bacterial 6-phosphogluconate dehydrogenase reveal aspects of specificity, mechanism and mode of inhibition by analogues of high-energy reaction intermediates., Sundaramoorthy R, Iulek J, Barrett MP, Bidet O, Ruda GF, Gilbert IH, Hunter WN, FEBS J. 2007 Jan;274(1):275-86. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17222187 17222187] | Crystal structures of a bacterial 6-phosphogluconate dehydrogenase reveal aspects of specificity, mechanism and mode of inhibition by analogues of high-energy reaction intermediates., Sundaramoorthy R, Iulek J, Barrett MP, Bidet O, Ruda GF, Gilbert IH, Hunter WN, FEBS J. 2007 Jan;274(1):275-86. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17222187 17222187] | ||
[[Category: Lactococcus lactis]] | [[Category: Lactococcus lactis]] | ||
| + | [[Category: Phosphogluconate dehydrogenase (decarboxylating)]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Hunter, W.N.]] | [[Category: Hunter, W.N.]] | ||
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[[Category: pentose shunt]] | [[Category: pentose shunt]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 12:48:49 2007'' |
Revision as of 10:44, 30 October 2007
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STRUCTURAL CHARACTERIZATION OF A BACTERIAL 6PDH REVEALS ASPECTS OF SPECIFICITY, MECHANISM AND MODE OF INHIBITION
Overview
Crystal structures of recombinant Lactococcus lactis 6-phosphogluconate, dehydrogenase (LlPDH) in complex with substrate, cofactor, product and, inhibitors have been determined. LlPDH shares significant sequence, identity with the enzymes from sheep liver and the protozoan parasite, Trypanosoma brucei for which structures have been reported. Comparisons, indicate that the key residues in the active site are highly conserved, as, are the interactions with the cofactor and the product ribulose, 5-phosphate. However, there are differences in the conformation of the, substrate 6-phosphogluconate which may reflect distinct states relevant to, catalysis. Analysis of the complex formed with the potent inhibitor, 4-phospho-d-erythronohydroxamic acid, suggests that this molecule does, indeed mimic ... [(full description)]
About this Structure
2IYO is a [Single protein] structure of sequence from [Lactococcus lactis] with 6PG and CAC as [ligands]. Active as [Phosphogluconate dehydrogenase (decarboxylating)], with EC number [1.1.1.44]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
Crystal structures of a bacterial 6-phosphogluconate dehydrogenase reveal aspects of specificity, mechanism and mode of inhibition by analogues of high-energy reaction intermediates., Sundaramoorthy R, Iulek J, Barrett MP, Bidet O, Ruda GF, Gilbert IH, Hunter WN, FEBS J. 2007 Jan;274(1):275-86. PMID:17222187
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