1BWZ

DIAMINOPIMELATE EPIMERASE FROM HEMOPHILUS INFLUENZAE

Summary for 1BWZ

• Entry DOI: 10.2210/pdb1bwz/pdb
• Descriptor: PROTEIN (DIAMINOPIMELATE EPIMERASE) (2 entities in total)
• Functional Keywords: metabolic role, structural classification, isomerase
• Biological source: Haemophilus influenzae
• Cellular location: Cytoplasm : P44859
• Total number of polymer chains: 1
• Total formula weight: 30295.58

Authors

Cirilli, M.,Zheng, R.,Scapin, G.,Blanchard, J.S. (deposition date: 1998-09-29, release date: 1998-12-16, Last modification date: 2024-11-20)

Primary citation

Cirilli, M.,Zheng, R.,Scapin, G.,Blanchard, J.S.
Structural symmetry: the three-dimensional structure of Haemophilus influenzae diaminopimelate epimerase.
Biochemistry, 37:16452-16458, 1998

PubMed Abstract: 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.

PubMed: 9843410
DOI: 10.1021/bi982138o

Experimental method

X-RAY DIFFRACTION (2.72 Å)