› 4pmn

X-ray diffraction
1.44Å resolution

Crystal structure of the Mycobacterium tuberculosis Tat-secreted protein Rv2525c in complex with MES (monoclinic crystal form I)

Released:
DOI: 10.2210/pdb4pmn/pdb
PDB entry 4pmn coloured by chain, front view.
PDB entry 4pmn coloured by chain, side view.
PDB entry 4pmn coloured by chain, top view.
Source organism: Mycobacterium tuberculosis CDC1551
Primary publication:
Structural studies suggest a peptidoglycan hydrolase function for the Mycobacterium tuberculosis Tat-secreted protein Rv2525c.
Bellinzoni M, Haouz A, Miras I, Magnet S, André-Leroux G, Mukherjee R, Shepard W, Cole ST, Alzari PM
J Struct Biol 188 156-64 (2014)
PMID: 25260828

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161142 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Rv2525c-like glycoside hydrolase-like domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 234 amino acids
Theoretical weight: 25.57 KDa
Source organism: Mycobacterium tuberculosis CDC1551
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P95028 (Residues: 36-240; Coverage: 85%)
Gene name: MT2601
Sequence domains: Rv2525c-like, glycoside hydrolase-like domain
Structure domains: Glycosidases

Ligands and Environments

3 bound ligands:
Ligand MES 2 x MES
Ligand GOL 1 x GOL
Ligand SO4 1 x SO4
1 modified residue:
Ligand MSE 4 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: C2
Unit cell:
a: 100.05Å b: 73.77Å c: 76.065Å
α: 90° β: 131.87° γ: 90°
R-values:
R R work R free
0.163 0.162 0.181
Expression system: Escherichia coli BL21

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Citations

5 citation in other articles

Rv0500A is a transcription factor that links Mycobacterium tuberculosis environmental response with division and impacts host colonization.
Kevorkian et al. (2022)
4 more