2ce3

X-ray diffraction
2.6Å resolution

CRYSTAL STRUCTURE OF THE ATP-DEPENDENT CLP PROTEASE PROTEOLYTIC SUBUNIT 1 (CLPP1) FROM MYCOBACTERIUM TUBERCULOSIS

Released:

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:

Structure analysis Details

Assembly composition:
homo tetradecamer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ATP-dependent Clp protease proteolytic subunit 1 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: 200 amino acids
Theoretical weight: 21.73 KDa
Source organism: Mycobacterium tuberculosis H37Rv
Expression system: Escherichia coli
UniProt:
  • Canonical: P9WPC5 (Residues: 1-200; Coverage: 100%)
Gene names: MTV008.17c, Rv2461c, clpP, clpP1
Sequence domains: Clp protease
Structure domains: 2-enoyl-CoA Hydratase; Chain A, domain 1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: P21
Unit cell:
a: 97.719Å b: 168.948Å c: 104.364Å
α: 90° β: 114.83° γ: 90°
R-values:
R R work R free
0.205 0.202 0.261
Expression system: Escherichia coli