› 7f71

X-ray diffraction
1.58Å resolution

Crystal structure of the Mycobacterium tuberculosis L,D-transpeptidase-2 (LdtMt2) with peptidoglycan sugar moiety and glutamate

Released:
DOI: 10.2210/pdb7f71/pdb
PDB entry 7f71 coloured by chain, front view.
PDB entry 7f71 coloured by chain, side view.
PDB entry 7f71 coloured by chain, top view.
Source organism: Mycobacterium tuberculosis H37Rv
Primary publication:
Allosteric cooperation in β-lactam binding to a non-classical transpeptidase.
Ahmad N, Dugad S, Chauhan V, Ahmed S, Sharma K, Kachhap S, Zaidi R, Bishai WR, Lamichhane G, Kumar P
Elife 11 (2022)
PMID: 35475970

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-125201 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L,D-transpeptidase 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 370 amino acids
Theoretical weight: 39.53 KDa
Source organism: Mycobacterium tuberculosis H37Rv
Expression system: Escherichia coli
UniProt:
  • Canonical: I6Y9J2 (Residues: 42-408; Coverage: 98%)
Gene names: P425_02624, RVBD_2518c, Rv2518c, ldtB, lppS
Sequence domains:

Ligands and Environments

3 bound ligands:
Ligand GOL 2 x GOL
Ligand GLU 2 x GLU
Ligand BGC 1 x BGC
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P21
Unit cell:
a: 60.906Å b: 93.981Å c: 75.539Å
α: 90° β: 92.975° γ: 90°
R-values:
R R work R free
0.166 0.165 0.198
Expression system: Escherichia coli

Quick links

Citations

1 citations in other articles

The l,d-Transpeptidase LdtAb from Acinetobacter baumannii Is Poorly Inhibited by Carbapenems and Has a Unique Structural Architecture.
Toth et al. (2022)

1 mention without citation

Allosteric cooperation in β-lactam binding to a non-classical transpeptidase.
Ahmad et al. (2022)