› 4ewl

X-ray diffraction
1.85Å resolution

Crystal Structure of MshB with glycerol and Acetate bound in the active site

Released:
DOI: 10.2210/pdb4ewl/pdb
PDB entry 4ewl coloured by chain, front view.
PDB entry 4ewl coloured by chain, side view.
PDB entry 4ewl coloured by chain, top view.
Source organism: Mycobacterium tuberculosis
Primary publication:
A new crystal form of MshB from Mycobacterium tuberculosis with glycerol and acetate in the active site suggests the catalytic mechanism.
Broadley SG, Gumbart JC, Weber BW, Marakalala MJ, Steenkamp DJ, Sewell BT
Acta Crystallogr D Biol Crystallogr 68 1450-9 (2012)
PMID: 23090394

Function and Biology Details

Reaction catalysed: 
1-O-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol + H(2)O = 1-O-(2-amino-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol + acetate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161704 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
1D-myo-inositol 2-acetamido-2-deoxy-alpha-D-glucopyranoside deacetylase Chains: A, B
Molecule details ›
Chains: A, B
Length: 299 amino acids
Theoretical weight: 31.46 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P9WJN3 (Residues: 1-299; Coverage: 99%)
Gene names: Rv1170, mshB
Sequence domains: GlcNAc-PI de-N-acetylase
Structure domains: LmbE-like

Ligands and Environments

4 bound ligands:
Ligand PE4 2 x PE4
Ligand GOL 9 x GOL
Ligand ZN 2 x ZN
Ligand ACT 2 x ACT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: C2
Unit cell:
a: 147.379Å b: 71.903Å c: 97.681Å
α: 90° β: 128.29° γ: 90°
R-values:
R R work R free
0.191 0.189 0.224
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Properties and biotechnological applications of microbial deacetylase.
Zou et al. (2023)
7 other articles

2 mentions without citation

Structure and function of the LmbE-like superfamily.
Viars et al. (2014)
1 more