› 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 7ocn coloured by chain and viewed from the front.
PDB 7ocn coloured by chain and viewed from the side.
PDB 7ocn coloured by chain and viewed from the top.
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, Konig P, Himpich S, Ngu ND, Abele R, Muller V, Pos KM
Proc. Natl. Acad. Sci. U.S.A. 119 e2107994119-e2107994119 (2022)
PMID: 35363566

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Mannitol dehydrogenase C-terminal domain-containing protein 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 names: HMPREF0010_00722, HTZ92_1619
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)

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