PDBsum entry 3v5e

Hydrolase

PDB id: 3v5e

Contents

Protein chains

(+ 8 more) 184 a.a.

Waters ×95

PDB id:

3v5e

Name:

Hydrolase

Title:

Crystal structure of clpp from staphylococcus aureus in the active, extended conformation

Structure:

Atp-dependent clp protease proteolytic subunit. Chain: a, b, c, d, e, f, g, h, i, j, k, l, m, n. Synonym: endopeptidase clp. Engineered: yes

Source:

Staphylococcus aureus subsp. Aureus. Organism_taxid: 93061. Strain: nctc 8325. Gene: clpp, saouhsc_00790. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

2.30Å R-factor: 0.202 R-free: 0.231

Authors:

M.Gersch,A.List,M.Groll,S.Sieber

Key ref:

M.Gersch et al. (2012). Insights into structural network responsible for oligomerization and activity of bacterial virulence regulator caseinolytic protease P (ClpP) protein. J Biol Chem, 287, 9484-9494. PubMed id: 22291011

Date:

16-Dec-11 Release date: 08-Feb-12

Protein chains

Q2G036  (CLPP_STAA8) -  ATP-dependent Clp protease proteolytic subunit from Staphylococcus aureus (strain NCTC 8325 / PS 47)

Seq: 195 a.a.

Struc: 184 a.a.

Enzyme reactions

• Enzyme class: E.C.3.4.21.92 - endopeptidase Clp.
• Reaction: Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. Alpha-casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are cleaved (such as succinyl-Leu-Tyr-|-NHMEC; and Leu-Tyr-Leu-|-Tyr-Trp, in which the cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp- bond also occurs).

J Biol Chem 287:9484-9494 (2012)

PubMed id: 22291011

Insights into structural network responsible for oligomerization and activity of bacterial virulence regulator caseinolytic protease P (ClpP) protein.

M.Gersch, A.List, M.Groll, S.A.Sieber.

ABSTRACT

No abstract given.