1geg: Difference between revisions
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|PDB= 1geg |SIZE=350|CAPTION= <scene name='initialview01'>1geg</scene>, resolution 1.7Å | |PDB= 1geg |SIZE=350|CAPTION= <scene name='initialview01'>1geg</scene>, resolution 1.7Å | ||
|SITE= | |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> | |LIGAND= <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=GLC:GLUCOSE'>GLC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene> | ||
|ACTIVITY= <span class='plainlinks'>[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] </span> | |||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1geg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1geg OCA], [http://www.ebi.ac.uk/pdbsum/1geg PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1geg RCSB]</span> | |||
}} | }} | ||
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[[Category: Otagiri, M.]] | [[Category: Otagiri, M.]] | ||
[[Category: Ui, S.]] | [[Category: Ui, S.]] | ||
[[Category: sdr family]] | [[Category: sdr family]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:42:21 2008'' | ||
Revision as of 17:42, 30 March 2008
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| 1geg, resolution 1.7Å | |||||||||||||
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| Ligands: | BME, GLC, MG, NAD | ||||||||||||
| Activity: | Acetoin dehydrogenase, with EC number 1.1.1.5 | ||||||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| 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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