› 4gsu

X-ray diffraction
2Å resolution

Structural basis for the inhibition of Mycobacterium tuberculosis L,D-transpeptidase by meropenem, a drug effective against extensively drug-resistant strains

Released:
DOI: 10.2210/pdb4gsu/pdb
PDB entry 4gsu coloured by chain, front view.
PDB entry 4gsu coloured by chain, side view.
PDB entry 4gsu coloured by chain, top view.
Source organism: Mycobacterium tuberculosis
Primary publication:
Structural basis for the inhibition of Mycobacterium tuberculosis L,D-transpeptidase by meropenem, a drug effective against extensively drug-resistant strains.
Kim HS, Kim J, Im HN, Yoon JY, An DR, Yoon HJ, Kim JY, Min HK, Kim SJ, Lee JY, Han BW, Suh SW
Acta Crystallogr D Biol Crystallogr 69 420-31 (2013)
PMID: 23519417

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-129428 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L,D-transpeptidase 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 287 amino acids
Theoretical weight: 31.28 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli
UniProt:
  • Canonical: O53223 (Residues: 131-408; Coverage: 74%)
Gene names: MT2594, V735_02606, ldtB
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand DWZ 2 x DWZ
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-1A
Spacegroup: P212121
Unit cell:
a: 68.937Å b: 73.433Å c: 104.071Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.186 0.232
Expression system: Escherichia coli

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Citations

6 review citations

Cell Wall Hydrolases in Bacteria: Insight on the Diversity of Cell Wall Amidases, Glycosidases and Peptidases Toward Peptidoglycan.
Vermassen et al. (2019)
5 more

11 mentions without citation

β-Lactam antibiotic targets and resistance mechanisms: from covalent inhibitors to substrates.
Mora-Ochomogo et al. (2021)
10 more