› 4zfq

X-ray diffraction
2.8Å resolution

Structure of M. tuberculosis (3,3) L,D-Transpeptidase, LdtMt5. (Meropenen-adduct form)

Released:
DOI: 10.2210/pdb4zfq/pdb
PDB entry 4zfq coloured by chain, front view.
PDB entry 4zfq coloured by chain, side view.
PDB entry 4zfq coloured by chain, top view.
Source organism: Mycobacterium tuberculosis CDC1551
Primary publication:
Loss of a Functionally and Structurally Distinct ld-Transpeptidase, LdtMt5, Compromises Cell Wall Integrity in Mycobacterium tuberculosis.
Brammer Basta LA, Ghosh A, Pan Y, Jakoncic J, Lloyd EP, Townsend CA, Lamichhane G, Bianchet MA
J Biol Chem 290 25670-85 (2015)
PMID: 26304120

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161756 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L,D-transpeptidase 5 Chain: A
Molecule details ›
Chain: A
Length: 451 amino acids
Theoretical weight: 47.93 KDa
Source organism: Mycobacterium tuberculosis CDC1551
Expression system: Escherichia coli
UniProt:
  • Canonical: P9WKV2 (Residues: 1-451; Coverage: 100%)
Gene name: MT0501
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand PEG 2 x PEG
Ligand DWZ 1 x DWZ
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X6A
Spacegroup: P6222
Unit cell:
a: 99.393Å b: 99.393Å c: 193.384Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.232 0.23 0.277
Expression system: Escherichia coli

Quick links

Citations

6 review citations

New Insights in to the Intrinsic and Acquired Drug Resistance Mechanisms in Mycobacteria.
Nasiri et al. (2017)
5 more

2 mentions without citation

Loss of a Functionally and Structurally Distinct ld-Transpeptidase, LdtMt5, Compromises Cell Wall Integrity in Mycobacterium tuberculosis.
Brammer Basta et al. (2015)
1 more