› 2l26

Solution NMR

Rv0899 from Mycobacterium tuberculosis contains two separated domains

Released:
DOI: 10.2210/pdb2l26/pdb
PDB entry 2l26 coloured by chain, ensemble of 10 models, front view.
PDB entry 2l26 coloured by chain, ensemble of 10 models, side view.
PDB entry 2l26 coloured by chain, ensemble of 10 models, top view.
Source organism: Mycobacterium tuberculosis H37Rv
Primary publication:
Structural studies of Mycobacterium tuberculosis Rv0899 reveal a monomeric membrane-anchoring protein with two separate domains.
Li J, Shi C, Gao Y, Wu K, Shi P, Lai C, Chen L, Wu F, Tian C
J Mol Biol 415 382-92 (2012)
PMID: 22108166

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161661 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidoglycan-binding protein ArfA Chain: A
Molecule details ›
Chain: A
Length: 284 amino acids
Theoretical weight: 29.44 KDa
Source organism: Mycobacterium tuberculosis H37Rv
Expression system: Escherichia coli
UniProt:
  • Canonical: P9WIU5 (Residues: 75-326; Coverage: 77%)
Gene names: MTCY31.27, Rv0899, arfA, ompA
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

4 citation in other articles

The non-catalytic "cap domain" of a mycobacterial metallophosphoesterase regulates its expression and localization in the cell.
Matange et al. (2014)
3 more

3 mentions without citation

Solution NMR Studies of Mycobacterium tuberculosis Proteins for Antibiotic Target Discovery.
Kim et al. (2017)
2 more