› 6naw

X-ray diffraction
2.4Å resolution

Crystal structure of Neisseria meningitidis ClpP E58A activated mutant

Released:
DOI: 10.2210/pdb6naw/pdb
PDB entry 6naw coloured by chain, front view.
PDB entry 6naw coloured by chain, side view.
PDB entry 6naw coloured by chain, top view.
Source organism: Neisseria meningitidis
Primary publication:
Mabanglo MF, Leung E, Vahidi S, Seraphim TV, Eger BT, Bryson S, Bhandari V, Zhou JL, Mao YQ, Rizzolo K, Barghash MM, Goodreid JD, Phanse S, Babu M, Barbosa LRS, Ramos CHI, Batey RA, Kay LE, Pai EF, Houry WA
Commun Biol
PMID: 31925204

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-191701 (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: 217 amino acids
Theoretical weight: 24.35 KDa
Source organism: Neisseria meningitidis
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9JZ38 (Residues: 1-204; Coverage: 100%)
Gene names: NMB1312, clpP
Sequence domains: Clp protease

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E SUPERBRIGHT
Spacegroup: P21
Unit cell:
a: 98.122Å b: 119.365Å c: 127.639Å
α: 90° β: 89.99° γ: 90°
R-values:
R R work R free
0.194 0.193 0.252
Expression system: Escherichia coli

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