PDBsum entry 5abk

Hydrolase

PDB id: 5abk

Contents

Protein chain

84 a.a.

PDB id:

5abk

Name:

Hydrolase

Title:

Structure of the n-terminal domain of the metalloprotease prtv from vibrio cholerae

Structure:

Metalloprotease. Chain: a. Fragment: n-terminal domain, unp residues 23-103. Synonym: metalloprotease prtv. Engineered: yes

Source:

Vibrio cholerae. Organism_taxid: 666. Expressed in: escherichia coli. Expression_system_taxid: 469008. Expression_system_variant: plyss.

NMR struc:

20 models

Authors:

C.Persson,M.Mayzel,A.Edwin,S.N.Wai,A.Ohman,A.E.Sauer-Eriksson, G.Karlsson

Key ref:

A.Edwin et al. (2015). Structure of the N-terminal domain of the metalloprotease PrtV from Vibrio cholerae. Protein Sci, 24, 2076-2080. PubMed id: 26434928 DOI: 10.1002/pro.2815

Date:

06-Aug-15 Release date: 26-Aug-15

Protein chain

Q9KMU6  (PRTV_VIBCH) -  Pre-pro-metalloprotease PrtV from Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)

Seq: 918 a.a.

Struc: 84 a.a.*

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.3.4.24.- - ?????

DOI no: 10.1002/pro.2815

Protein Sci 24:2076-2080 (2015)

PubMed id: 26434928

Structure of the N-terminal domain of the metalloprotease PrtV from Vibrio cholerae.

A.Edwin, C.Persson, M.Mayzel, S.N.Wai, A.Öhman, B.G.Karlsson, A.E.Sauer-Eriksson.

ABSTRACT

The metalloprotease PrtV from Vibrio cholerae serves an important function for the ability of bacteria to invade the mammalian host cell. The protein belongs to the family of M6 proteases, with a characteristic zinc ion in the catalytic active site. PrtV constitutes a 918 amino acids (102 kDa) multidomain pre-pro-protein that undergoes several N- and C-terminal modifications to form a catalytically active protease. We report here the NMR structure of the PrtV N-terminal domain (residues 23-103) that contains two short α-helices in a coiled coil motif. The helices are held together by a cluster of hydrophobic residues. Approximately 30 residues at the C-terminal end, which were predicted to form a third helical structure, are disordered. These residues are highly conserved within the genus Vibrio, which suggests that they might be functionally important.