1FNO

PEPTIDASE T (TRIPEPTIDASE)

Summary for 1FNO

• Entry DOI: 10.2210/pdb1fno/pdb
• Descriptor: PEPTIDASE T, ZINC ION, SULFATE ION, ... (4 entities in total)
• Functional Keywords: metallo peptidase, protease, hydrolase
• Biological source: Salmonella typhimurium
• Cellular location: Cytoplasm: P26311
• Total number of polymer chains: 1
• Total formula weight: 47002.72

Authors

Hakansson, K.,Miller, C.G. (deposition date: 2000-08-22, release date: 2002-03-13, Last modification date: 2024-11-13)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.4 Å)