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Structure paper

TitleUnidirectional mannitol synthesis of Acinetobacter baumannii MtlD is facilitated by the helix-loop-helix-mediated dimer formation.
Journal, issue, pagesProc. Natl. Acad. Sci. USA, Vol. 119, Page e2107994119-e2107994119, Year 2022
Publish dateApr 28, 2021 (structure data deposition date)
AuthorsTam, H.K. / Konig, P. / Himpich, S. / Ngu, N.D. / Abele, R. / Muller, V. / Pos, K.M.
External linksProc. Natl. Acad. Sci. USA / PubMed:35363566
MethodsX-ray diffraction
Resolution2.3 - 2.9 Å
Structure data

PDB-7ocn:
Crystal structure of the bifunctional mannitol-1-phosphate dehydrogenase/phosphatase MtlD from Acinetobacter baumannii
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

PDB-7ocp:
NADPH bound to the dehydrogenase domain of the bifunctional mannitol-1-phosphate dehydrogenase/phosphatase MtlD from Acinetobacter baumannii
Method: X-RAY DIFFRACTION / Resolution: 2.75 Å

PDB-7ocq:
NADH bound to the dehydrogenase domain of the bifunctional mannitol-1-phosphate dehydrogenase/phosphatase MtlD from Acinetobacter baumannii
Method: X-RAY DIFFRACTION / Resolution: 2.9 Å

PDB-7ocr:
NADPH and fructose-6-phosphate bound to the dehydrogenase domain of the bifunctional mannitol-1-phosphate dehydrogenase/phosphatase MtlD from Acinetobacter baumannii
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

PDB-7ocs:
Mannitol-1-phosphate bound to the phosphatase domain of the bifunctional mannitol-1-phosphate dehydrogenase/phosphatase MtlD-D16A from Acinetobacter baumannii
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

PDB-7oct:
NADPH bound to the dehydrogenase domain of the bifunctional mannitol-1-phosphate dehydrogenase/phosphatase MtlD-N374A from Acinetobacter baumannii
Method: X-RAY DIFFRACTION / Resolution: 2.85 Å

PDB-7ocu:
Mannitol-1-phosphate bound to the phosphatase domain of the bifunctional mannitol-1-phosphate dehydrogenase/phosphatase MtlD-N374A from Acinetobacter baumannii
Method: X-RAY DIFFRACTION / Resolution: 2.7 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-SO4:
SULFATE ION

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-CL:
Unknown entry

ChemComp-BR:
BROMIDE ION

ChemComp-EPE:
4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID / pH buffer*YM

ChemComp-HOH:
WATER

ChemComp-NDP:
NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE

ChemComp-V8H:
[[(2~{R},3~{S},4~{R},5~{R})-5-(3-aminocarbonyl-4~{H}-pyridin-1-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] [(2~{R},3~{S},4~{R},5~{R})-3,4,5-tris(oxidanyl)oxolan-2-yl]methyl hydrogen phosphate

ChemComp-GOL:
GLYCEROL

ChemComp-NAI:
1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE

ChemComp-K:
Unknown entry

ChemComp-F6R:
FRUCTOSE -6-PHOSPHATE

ChemComp-PGE:
TRIETHYLENE GLYCOL

ChemComp-PG4:
TETRAETHYLENE GLYCOL / precipitant*YM

ChemComp-BME:
BETA-MERCAPTOETHANOL

ChemComp-44H:
D-Mannitol-1-phosphate

ChemComp-NA:
Unknown entry

ChemComp-ACT:
ACETATE ION

Source
  • acinetobacter baumannii (strain atcc 19606 / dsm 30007 / cip 70.34 / jcm 6841 / nbrc 109757 / ncimb 12457 / nctc 12156 / 81) (bacteria)
  • acinetobacter baumannii atcc 19606 = cip 70.34 = jcm 6841 (bacteria)
KeywordsOXIDOREDUCTASE / Mannitol / Dehydrogenase / Phosphatase / NADPH / Fructose-6-phosphate / HAD hydrolase family IA variant 3

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