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1geg

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{{STRUCTURE_1geg| PDB=1geg | SCENE= }}
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'''CRYATAL STRUCTURE ANALYSIS OF MESO-2,3-BUTANEDIOL DEHYDROGENASE'''
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===CRYATAL STRUCTURE ANALYSIS OF MESO-2,3-BUTANEDIOL DEHYDROGENASE===
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==Overview==
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The crystal structure of a ternary complex of meso-2,3-butanediol dehydrogenase with NAD+ and a competitive inhibitor, mercaptoethanol, has been determined at 1.7 A resolution by means of molecular replacement and refined to a final R-factor of 0.194. The overall structure is similar to those of the other short chain dehydrogenase/reductase enzymes. The NAD+ binding site, and the positions of catalytic residues Ser139, Tyr152, and Lys156 are also conserved. The crystal structure revealed that mercaptoethanol bound specifically to meso-2,3-butanediol dehydrogenase. Two residues around the active site, Gln140 and Gly183, forming hydrogen bonds with the inhibitor, are important but not sufficient for distinguishing stereoisomerism of a chiral substrate.
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(as it appears on PubMed at http://www.pubmed.gov), where 11173520 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11173520}}
==About this Structure==
==About this Structure==
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[[Category: Ui, S.]]
[[Category: Ui, S.]]
[[Category: Sdr family]]
[[Category: Sdr family]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:28:19 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 05:10:15 2008''

Revision as of 02:10, 1 July 2008

Image:1geg.png

Template:STRUCTURE 1geg

CRYATAL STRUCTURE ANALYSIS OF MESO-2,3-BUTANEDIOL DEHYDROGENASE

Template:ABSTRACT PUBMED 11173520

About this Structure

1GEG is a Single protein structure of sequence from Klebsiella pneumoniae. Full crystallographic information is available from OCA.

Reference

Crystal structure of meso-2,3-butanediol dehydrogenase in a complex with NAD+ and inhibitor mercaptoethanol at 1.7 A resolution for understanding of chiral substrate recognition mechanisms., Otagiri M, Kurisu G, Ui S, Takusagawa Y, Ohkuma M, Kudo T, Kusunoki M, J Biochem. 2001 Feb;129(2):205-8. PMID:11173520

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