7ocr

NADPH and fructose-6-phosphate bound to the dehydrogenase domain of the bifunctional mannitol-1-phosphate dehydrogenase/phosphatase MtlD from Acinetobacter baumannii

spinqualitylabelsall models 7ocr, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7ocr is a 2 chain structure with sequence from Acinetobacter baumannii ATCC 19606 = CIP 70.34 = JCM 6841. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.6Å Ligands: CL, EDO, EPE, F6R, K, MG, NDP, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function D0C7J2_ACIB2 Publication Abstract from PubMed SignificanceMannitol biosynthesis is essential for Acinetobacter baumannii to cope with osmotic stress. Currently, only Pseudomonas putida, Acinetobacter baylyi, and A. baumannii are able to de novo synthesize mannitol by a structurally unique bifunctional mannitol-1-phosphate dehydrogenase/phosphatase (AbMtlD). The molecular mechanism of reduction and dephosphorylation of fructose-6-phosphate to mannitol is highly dependent on the substrate shuffling from one protomer to the other protomer by a unique helix-loop-helix domain-mediated dimer formation, thus ensuring unidirectional and efficient biosynthesis of mannitol. These observations support an evolutionary adaptation of AbMtlD by fusion of dehydrogenase and phosphatase domains to facilitate efficient unidirectional enzymatic production of mannitol, unifying regulatory control and minimizing the intracellular concentration of toxic mannitol-1-phosphate during salt stress. 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. 2022 Apr 5;119(14):e2107994119. doi:, 10.1073/pnas.2107994119. Epub 2022 Apr 1. PMID:35363566 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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