1bg6
From Proteopedia
CRYSTAL STRUCTURE OF THE N-(1-D-CARBOXYLETHYL)-L-NORVALINE DEHYDROGENASE FROM ARTHROBACTER SP. STRAIN 1C
Overview
Opine dehydrogenases catalyze the NAD(P)H-dependent reversible reaction to form opines that contain two asymmetric centers exhibiting either (L,L) or (D,L) stereochemistry. The first structure of a (D,L) superfamily member, N-(1-D-carboxylethyl)-L-norvaline dehydrogenase (CENDH) from Arthrobacter sp. strain 1C, has been determined at 1.8 A resolution and the location of the bound nucleotide coenzyme has been identified. Six conserved residues cluster in the cleft between the enzyme's two domains, close to the nucleotide binding site, and are presumed to define the enzyme's catalytic machinery. Conservation of a His-Asp pair as part of this cluster suggests that the enzyme mechanism is related to the 2-hydroxy acid dehydrogenases. The pattern of sequence conservation and substitution between members of this enzyme family has permitted the tentative location of the residues that define their differential substrate specificities.
About this Structure
1BG6 is a Single protein structure of sequence from Arthrobacter. Full crystallographic information is available from OCA.
Reference
Crystal structure and active site location of N-(1-D-carboxylethyl)-L-norvaline dehydrogenase., Britton KL, Asano Y, Rice DW, Nat Struct Biol. 1998 Jul;5(7):593-601. PMID:9665174 Page seeded by OCA on Fri May 2 11:28:26 2008
