› 6ewy

X-ray diffraction
2.2Å resolution

RipA Peptidoglycan hydrolase (Rv1477, Mycobacterium tuberculosis) N-terminal domain

Released:
DOI: 10.2210/pdb6ewy/pdb
PDB entry 6ewy coloured by chain, front view.
PDB entry 6ewy coloured by chain, side view.
PDB entry 6ewy coloured by chain, top view.
Source organism: Mycobacterium tuberculosis H37Rv
Primary publication:
The Structure of the N-terminal Module of the Cell Wall Hydrolase RipA and its Role in Regulating Catalytic Activity.
Steiner EM, Lyngs�� J, Guy JE, Bourenkov G, Lindqvist Y, Schneider TR, Pedersen JS, Schneider G, Schnell R
Proteins (2018)
PMID: 29722065

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-129424 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidoglycan endopeptidase RipA Chain: A
Molecule details ›
Chain: A
Length: 219 amino acids
Theoretical weight: 23.27 KDa
Source organism: Mycobacterium tuberculosis H37Rv
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O53168 (Residues: 39-255; Coverage: 50%)
Gene names: Rv1477, ripA

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: C222
Unit cell:
a: 44.916Å b: 93.96Å c: 138.672Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.23 0.228 0.267
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Peptidoglycan NlpC/P60 peptidases in bacterial physiology and host interactions.
Griffin et al. (2023)
9 other articles

2 mentions without citation

The Cell Wall Hydrolytic NlpC/P60 Endopeptidases in Mycobacterial Cytokinesis: A Structural Perspective.
Squeglia et al. (2019)
1 more