1xdw
From Proteopedia
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- | [[Image:1xdw.gif|left|200px]] | + | [[Image:1xdw.gif|left|200px]] |
- | + | ||
- | '''NAD+-dependent (R)-2-Hydroxyglutarate Dehydrogenase from Acidaminococcus fermentans''' | + | {{Structure |
+ | |PDB= 1xdw |SIZE=350|CAPTION= <scene name='initialview01'>1xdw</scene>, resolution 1.98Å | ||
+ | |SITE= | ||
+ | |LIGAND= | ||
+ | |ACTIVITY= | ||
+ | |GENE= hgh ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=905 Acidaminococcus fermentans]) | ||
+ | }} | ||
+ | |||
+ | '''NAD+-dependent (R)-2-Hydroxyglutarate Dehydrogenase from Acidaminococcus fermentans''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1XDW is a [ | + | 1XDW is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Acidaminococcus_fermentans Acidaminococcus fermentans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XDW OCA]. |
==Reference== | ==Reference== | ||
- | Structural basis for stereo-specific catalysis in NAD(+)-dependent (R)-2-hydroxyglutarate dehydrogenase from Acidaminococcus fermentans., Martins BM, Macedo-Ribeiro S, Bresser J, Buckel W, Messerschmidt A, FEBS J. 2005 Jan;272(1):269-81. PMID:[http:// | + | Structural basis for stereo-specific catalysis in NAD(+)-dependent (R)-2-hydroxyglutarate dehydrogenase from Acidaminococcus fermentans., Martins BM, Macedo-Ribeiro S, Bresser J, Buckel W, Messerschmidt A, FEBS J. 2005 Jan;272(1):269-81. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15634349 15634349] |
[[Category: Acidaminococcus fermentans]] | [[Category: Acidaminococcus fermentans]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: structural variant of the bab rossmann fold]] | [[Category: structural variant of the bab rossmann fold]] | ||
- | ''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 15:08:30 2008'' |
Revision as of 13:08, 20 March 2008
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, resolution 1.98Å | |||||||
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Gene: | hgh (Acidaminococcus fermentans) | ||||||
Coordinates: | save as pdb, mmCIF, xml |
NAD+-dependent (R)-2-Hydroxyglutarate Dehydrogenase from Acidaminococcus fermentans
Overview
NAD(+)-dependent (R)-2-hydroxyglutarate dehydrogenase (HGDH) catalyses the reduction of 2-oxoglutarate to (R)-2-hydroxyglutarate and belongs to the d-2-hydroxyacid NAD(+)-dependent dehydrogenase (d-2-hydroxyacid dehydrogenase) protein family. Its crystal structure was determined by phase combination to 1.98 A resolution. Structure-function relationships obtained by the comparison of HGDH with other members of the d-2-hydroxyacid dehydrogenase family give a chemically satisfying view of the substrate stereoselectivity and catalytic requirements for the hydride transfer reaction. A model for substrate recognition and turnover is discussed. The HGDH active site architecture is structurally optimized to recognize and bind the negatively charged substrate 2-oxoglutarate. The structural position of the side chain of Arg52, and its counterparts in other family members, strongly correlates with substrate specificity towards substitutions at the C3 atom (linear or branched substrates). Arg235 interacts with the substrate's alpha-carboxylate and carbonyl groups, having a dual role in both substrate binding and activation, and the gamma-carboxylate group can dock at an arginine cluster. The proton-relay system built up by Glu264 and His297 permits His297 to act as acid-base catalyst and the 4Re-hydrogen from NADH is transferred as hydride to the carbonyl group Si-face leading to the formation of the correct enantiomer (R)-2-hydroxyglutarate.
About this Structure
1XDW is a Protein complex structure of sequences from Acidaminococcus fermentans. Full crystallographic information is available from OCA.
Reference
Structural basis for stereo-specific catalysis in NAD(+)-dependent (R)-2-hydroxyglutarate dehydrogenase from Acidaminococcus fermentans., Martins BM, Macedo-Ribeiro S, Bresser J, Buckel W, Messerschmidt A, FEBS J. 2005 Jan;272(1):269-81. PMID:15634349
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