1geg: Difference between revisions
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[[Image:1geg.jpg|left|200px]] | [[Image:1geg.jpg|left|200px]] | ||
'''CRYATAL STRUCTURE ANALYSIS OF MESO-2,3-BUTANEDIOL DEHYDROGENASE''' | {{Structure | ||
|PDB= 1geg |SIZE=350|CAPTION= <scene name='initialview01'>1geg</scene>, resolution 1.7Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=GLC:GLUCOSE'>GLC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene> and <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Acetoin_dehydrogenase Acetoin dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.5 1.1.1.5] | |||
|GENE= | |||
}} | |||
'''CRYATAL STRUCTURE ANALYSIS OF MESO-2,3-BUTANEDIOL DEHYDROGENASE''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1GEG is a [ | 1GEG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Klebsiella_pneumoniae Klebsiella pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GEG OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11173520 11173520] | ||
[[Category: Acetoin dehydrogenase]] | [[Category: Acetoin dehydrogenase]] | ||
[[Category: Klebsiella pneumoniae]] | [[Category: Klebsiella pneumoniae]] | ||
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[[Category: sdr family]] | [[Category: sdr family]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:21:59 2008'' | ||
Revision as of 09:22, 20 March 2008
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| 1geg, resolution 1.7Å | |||||||||||||
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| Ligands: | GLC, MG, NAD and BME | ||||||||||||
| Activity: | Acetoin dehydrogenase, with EC number 1.1.1.5 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
CRYATAL STRUCTURE ANALYSIS OF MESO-2,3-BUTANEDIOL DEHYDROGENASE
Overview
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.
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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