Brand  (β version)

PDB ID: 3KTK

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Ligands
Code Name Style Show Link
Non-standard Residues
Code Name Show
MAA N-methyl-L-alanine
MP8 (4r)-4-methyl-L-proline
WFP 3,5-difluoro-L-phenylalanine
YCP (2s)-piperidine-2-carboxylic acid
Glycosylation
Code Name Emphasize
Modification
Code Name Show
CXP Cyclohexane propionic acid
OTT (2e,4e,6e)-octa-2,4,6-trienoic acid

Structure summary

Code : 3KTK   PDBj   RCSB PDB   PDBe
Header : HYDROLASE/ANTIBIOTIC
Title : Structure of ClpP in complex with ADEP2 in triclinic crystal form
Release Data : 2010-03-23
Compound :
mol_id molecule chains synonym
1 ATP-dependent Clp protease proteolytic subunit A,B,C,D,E,F,G,H,I,J,K,L,M,N Endopeptidase Clp, Caseinolytic protease, Stress protein G7
ec: 3.4.21.92
mol_id molecule chains synonym
2 Acyldepsipeptide 2 O,P,Q,R,S,T,U,V,W,X,Y,Z,0,1 ADEP2
Source :
mol_id organism_scientific expression_system
1 Bacillus subtilis  (taxid:1423) Escherichia coli  (taxid:562)
gene: clpP, yvdN, BSU34540
expression_system_strain: BL21(DE3)
expression_system_vector_type: plasmid
expression_system_plasmid: pET26
mol_id organism_scientific
2 Synthetic
synthetic: yes
other_details: designed peptide based on ADEP1
Authors : Lee, B.-G., Brotz-Oesterhelt, H., Song, H.K.
Keywords : hydrolase, Protease, Serine protease, Stress response, A54556A, enopeptin, depsipeptide, antibiotics, HYDROLASE-ANTIBIOTIC complex
Exp. method : X-RAY DIFFRACTION ( 2.600 Å )
Citation :

Structures of ClpP in complex with acyldepsipeptide antibiotics reveal its activation mechanism

Lee, B.-G.,Park, E.Y.,Lee, K.-E.  et al.
(2010)  Nat.Struct.Mol.Biol.  17 : 471 - 478

PubMed: 20305655
DOI: 10.1038/nsmb.1787

Reaction

Chain : A, B, C, D, E, F, G, H, I, J, K, L, M, N
UniProt : P80244 (CLPP_BACSU)
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, PubMed:20305655
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