› 7ocn

X-ray diffraction
2.6Å resolution

Crystal structure of the bifunctional mannitol-1-phosphate dehydrogenase/phosphatase MtlD from Acinetobacter baumannii

Released:
DOI: 10.2210/pdb7ocn/pdb
PDB entry 7ocn coloured by chain, front view.
PDB entry 7ocn coloured by chain, side view.
PDB entry 7ocn coloured by chain, top view.
Source organism: Acinetobacter baumannii ATCC 19606 = CIP 70.34 = JCM 6841
Primary publication:
Unidirectional mannitol synthesis of Acinetobacter baumannii MtlD is facilitated by the helix-loop-helix-mediated dimer formation.
Tam HK, König P, Himpich S, Ngu ND, Abele R, Müller V, Pos KM
Proc Natl Acad Sci U S A 119 e2107994119 (2022)
PMID: 35363566

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-111919 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
HAD hydrolase, family IA, variant 3 Chains: A, B
Molecule details ›
Chains: A, B
Length: 727 amino acids
Theoretical weight: 83.55 KDa
Source organism: Acinetobacter baumannii ATCC 19606 = CIP 70.34 = JCM 6841
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: D0C7J2 (Residues: 2-715; Coverage: 100%)
Gene name: HMPREF0010_00722
Sequence domains:

Ligands and Environments

6 bound ligands:
Ligand MG 3 x MG
Ligand SO4 4 x SO4
Ligand EDO 2 x EDO
Ligand CL 4 x CL
Ligand BR 1 x BR
Ligand EPE 1 x EPE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 2
Spacegroup: C2221
Unit cell:
a: 99.496Å b: 157.418Å c: 219.802Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.238 0.237 0.267
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 citation in other articles

In-depth analysis of erythrose reductase homologs in Yarrowia lipolytica.
Szczepańczyk et al. (2023)
1 more