1bwz
From Proteopedia
DIAMINOPIMELATE EPIMERASE FROM HEMOPHILUS INFLUENZAE
Overview
The Haemophilus influenzae diaminopimelate epimerase was cloned, expressed, purified, and crystallized in the C2221 space group (a = 102.1 A, b = 115.4 A, c = 66.3 A, alpha = beta = gamma = 90 degrees). The three-dimensional structure was solved to 2.7 A using a single Pt derivative and the Se-Met-substituted enzyme to a conventional R factor of 19.0% (Rfree = 24.2%). The 274 amino acid enzyme consists of two structurally homologous domains, each containing eight beta-strands and two alpha-helices. Diaminopimelate epimerase is a representative of the PLP-independent amino acid racemases, for which no structure has yet been determined and substantial evidence exists supporting the role of two cysteine residues as the catalytic acid and base. Cys73 of the amino terminal domain is found in disulfide linkage, at the domain interface, with Cys217 of the carboxy terminal domain, and we suggest that these two cysteine residues in the reduced, active enzyme function as the acid and base in the mechanism.
About this Structure
1BWZ is a Single protein structure of sequence from Haemophilus influenzae. Full crystallographic information is available from OCA.
Reference
Structural symmetry: the three-dimensional structure of Haemophilus influenzae diaminopimelate epimerase., Cirilli M, Zheng R, Scapin G, Blanchard JS, Biochemistry. 1998 Nov 24;37(47):16452-8. PMID:9843410 Page seeded by OCA on Fri May 2 12:03:39 2008
