1FNO

PEPTIDASE T (TRIPEPTIDASE)

1FNO の概要

• エントリーDOI: 10.2210/pdb1fno/pdb
• 分子名称: PEPTIDASE T, ZINC ION, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: metallo peptidase, protease, hydrolase
• 由来する生物種: Salmonella typhimurium
• 細胞内の位置: Cytoplasm: P26311
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 47002.72

構造登録者

Hakansson, K.,Miller, C.G. (登録日: 2000-08-22, 公開日: 2002-03-13, 最終更新日: 2024-11-13)

主引用文献

Hakansson, K.,Miller, C.G.
Structure of Peptidase T from Salmonella typhimurium
Eur.J.Biochem., 269:443-450, 2002

PubMed Abstract: The structure of peptidase T, or tripeptidase, was determined by multiple wavelength anomalous dispersion (MAD) methodology and refined to 2.4 A resolution. Peptidase T comprises two domains; a catalytic domain with an active site containing two metal ions, and a smaller domain formed through a long insertion into the catalytic domain. The two metal ions, presumably zinc, are separated by 3.3 A, and are coordinated by five carboxylate and histidine ligands. The molecular surface of the active site is negatively charged. Peptidase T has the same basic fold as carboxypeptidase G2. When the structures of the two enzymes are superimposed, a number of homologous residues, not evident from the sequence alone, could be identified. Comparison of the active sites of peptidase T, carboxypeptidase G2, Aeromonas proteolytica aminopeptidase, carboxypeptidase A and leucine aminopeptidase reveals a common structural framework with interesting similarities and differences in the active sites and in the zinc coordination. A putative binding site for the C-terminal end of the tripeptide substrate was found at a peptidase T specific fingerprint sequence motif.

PubMed: 11856302
DOI: 10.1046/j.0014-2956.2001.02665.x

実験手法

X-RAY DIFFRACTION (2.4 Å)