Brand  (β version)

PDB ID: 5VZ2

Hetero Atom Contents

  The number of atoms exceeds 100,000.
  So, it can not be displayed here.

Select unit:

Select chain:   Sequence  

Data format:   

Color scheme of protein:

Ligands
Code Name Style Show Link
Non-standard Residues
Code Name Show
MP8 (4r)-4-methyl-L-proline
YCP (2s)-piperidine-2-carboxylic acid
Glycosylation
Code Name Emphasize
Modification
Code Name Show
9TS (2e)-pent-2-enoic acid

Structure summary

Code : 5VZ2   PDBj   RCSB PDB   PDBe
Header : HYDROLASE/ANTIBIOTIC
Title : Structure of ClpP from Staphylococcus aureus in complex with Acyldepsipeptide
Release Data : 2017-06-21
Compound :
mol_id molecule chains synonym
1 ATP-dependent Clp protease proteolytic subunit A,B,C,D,E,F,G,I,K,L,M,N,S,T Endopeptidase Clp
ec: 3.4.21.92
mol_id molecule chains
2 Acyldepsipeptide H,J,O,P,Q,R,U,V,X,Y,Z,a,b,c
Source :
mol_id organism_scientific expression_system
1 Staphylococcus aureus (strain NCTC 8325)  (taxid:93061) Escherichia coli BL21(DE3)  (taxid:469008)
strain: NCTC 8325
gene: clpP, SAOUHSC_00790
expression_system_strain: BL21 (DE3)
expression_system_plasmid: pET28a
mol_id organism_scientific
2 Synthetic construct  (taxid:32630)
synthetic: yes
Authors : Griffith, E.C., Lee, R.E.
Keywords : ClpP ADEP, HYDROLASE-ANTIBIOTIC complex
Exp. method : X-RAY DIFFRACTION ( 2.2600 Å )
Citation :

Ureadepsipeptides as ClpP Activators.

Griffith, E.C.,Zhao, Y.,Singh, A.P.  et al.
(2019)  Acs Infect Dis. 

PubMed: 31588734
DOI: 10.1021/acsinfecdis.9b00245

Structural switching of Staphylococcus aureus Clp protease: a key to understanding protease dynamics.

Zhang, J.,Ye, F.,Lan, L.  et al.
(2011)  J. Biol. Chem.  286 : 37590 - 37601

PubMed: 21900233
DOI: 10.1074/jbc.M111.277848

Acyldepsipeptide antibiotics induce the formation of a structured axial channel in ClpP: A model for the ClpX/ClpA-bound state of ClpP.

Li, D.H.,Chung, Y.S.,Gloyd, M.  et al.
(2010)  Chem. Biol.  17 : 959 - 969

PubMed: 20851345
DOI: 10.1016/j.chembiol.2010.07.008

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

Gersch, M.,List, A.,Groll, M.  et al.
(2012)  J. Biol. Chem.  287 : 9484 - 9494

PubMed: 22291011
DOI: 10.1074/jbc.M111.336222

Reaction

Chain : A, B, C, D, E, F, G, I, K, L, M, N, S, T
UniProt : Q2G036 (CLPP_STAA8)
Reaction: EC: Evidence:
Physiological Direction:
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 hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec, and Leu-Tyr-Leu-|-Tyr- Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs). 3.4.21.92 HAMAP-Rule:MF_00444
-