1BWZ

DIAMINOPIMELATE EPIMERASE FROM HEMOPHILUS INFLUENZAE

1BWZ の概要

• エントリーDOI: 10.2210/pdb1bwz/pdb
• 分子名称: PROTEIN (DIAMINOPIMELATE EPIMERASE) (2 entities in total)
• 機能のキーワード: metabolic role, structural classification, isomerase
• 由来する生物種: Haemophilus influenzae
• 細胞内の位置: Cytoplasm : P44859
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 30295.58

構造登録者

Cirilli, M.,Zheng, R.,Scapin, G.,Blanchard, J.S. (登録日: 1998-09-29, 公開日: 1998-12-16, 最終更新日: 2024-11-20)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.72 Å)