2iz1

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(New page: 200px<br /> <applet load="2iz1" size="450" color="white" frame="true" align="right" spinBox="true" caption="2iz1, resolution 2.30&Aring;" /> '''6PDH COMPLEXED WITH...)
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==About this Structure==
==About this Structure==
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2IZ1 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 CL, ATR, RES, P33 and PEG 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=2IZ1 OCA]].
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2IZ1 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 CL, ATR, RES, P33 and PEG 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=2IZ1 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]]
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[[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]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 17:13:33 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 11:02:32 2007''

Revision as of 08:57, 30 October 2007


2iz1, resolution 2.30Å

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6PDH COMPLEXED WITH PEX INHIBITOR SYNCHROTRON DATA

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

2IZ1 is a [Single protein] structure of sequence from [Lactococcus lactis] with CL, ATR, RES, P33 and PEG 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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