› 3q7h

X-ray diffraction
2.5Å resolution

Structure of the ClpP subunit of the ATP-dependent Clp Protease from Coxiella burnetii

Released:
DOI: 10.2210/pdb3q7h/pdb
PDB entry 3q7h coloured by chain, front view.
PDB entry 3q7h coloured by chain, side view.
PDB entry 3q7h coloured by chain, top view.
Source organism: Coxiella burnetii RSA 331
Entry authors: Anderson SM, Wawrzak Z, Gordon E, Hasseman J, Anderson WF, Savchenko A, Center for Structural Genomics of Infectious Diseases (CSGID)

Function and Biology Details

Reaction catalysed: 
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).
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetradecamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-182928 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ATP-dependent Clp protease proteolytic subunit Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N
Length: 195 amino acids
Theoretical weight: 21.96 KDa
Source organism: Coxiella burnetii RSA 331
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q83DJ2 (Residues: 1-195; Coverage: 100%)
Gene names: CBU_0738, clpP
Sequence domains: Clp protease
Structure domains: 2-enoyl-CoA Hydratase; Chain A, domain 1

Ligands and Environments

2 bound ligands:
Ligand PEG 33 x PEG
Ligand CA 28 x CA
1 modified residue:
Ligand MSE 98 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-D
Spacegroup: P21
Unit cell:
a: 101.912Å b: 137.469Å c: 127.784Å
α: 90° β: 109.03° γ: 90°
R-values:
R R work R free
0.172 0.17 0.208
Expression system: Escherichia coli BL21(DE3)

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