This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1dxy
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /> <applet load="1dxy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dxy, resolution 1.86Å" /> '''STRUCTURE OF D-2-HY...)
Next diff →
Revision as of 17:18, 29 October 2007
|
STRUCTURE OF D-2-HYDROXYISOCAPROATE DEHYDROGENASE
Overview
D-2-hydroxyisocaproate dehydrogenase (D-HicDH) from Lactobacillus casei is, a homodimer with 333 amino acids and a molecular mass of 37 kDa per, subunit. The enzyme belongs to the protein family of NAD+-dependent, D-2-hydroxycarboxylate dehydrogenases and within this family to the, subgroup of D-lactate dehydrogenases (D-LDHs). Compared with other D-LDHs, D-HicDH is characterized by a very low specificity regarding size and, chemical constitution of the accepted D-2-hydroxycarboxylates. Hexagonal, crystals of recombinant D-HicDH in the presence of NAD+ and, 2-oxoisocaproate (4-methyl-2-oxopentanoate) were grown with ammonium, sulphate as precipitating agent. The structure of these crystals was, solved by molecular replacement and refined to a final R-factor of 19.6%, for all measured ... [(full description)]
About this Structure
1DXY is a [Single protein] structure of sequence from [Lactobacillus casei] with SO4, NAD and COI as [ligands]. Full crystallographic information is available from [OCA].
Reference
Crystal structure of a ternary complex of D-2-hydroxyisocaproate dehydrogenase from Lactobacillus casei, NAD+ and 2-oxoisocaproate at 1.9 A resolution., Dengler U, Niefind K, Kiess M, Schomburg D, J Mol Biol. 1997 Apr 4;267(3):640-60. PMID:9126843
Page seeded by OCA on Mon Oct 29 19:22:49 2007
