7ocq
From Proteopedia
(Difference between revisions)
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==NADH bound to the dehydrogenase domain of the bifunctional mannitol-1-phosphate dehydrogenase/phosphatase MtlD from Acinetobacter baumannii== | ==NADH bound to the dehydrogenase domain of the bifunctional mannitol-1-phosphate dehydrogenase/phosphatase MtlD from Acinetobacter baumannii== | ||
| - | <StructureSection load='7ocq' size='340' side='right'caption='[[7ocq]]' scene=''> | + | <StructureSection load='7ocq' size='340' side='right'caption='[[7ocq]], [[Resolution|resolution]] 2.90Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7OCQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7OCQ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7ocq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Acinetobacter_baumannii_ATCC_19606_=_CIP_70.34_=_JCM_6841 Acinetobacter baumannii ATCC 19606 = CIP 70.34 = JCM 6841]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7OCQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7OCQ FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7ocq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ocq OCA], [https://pdbe.org/7ocq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ocq RCSB], [https://www.ebi.ac.uk/pdbsum/7ocq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ocq ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAI:1,4-DIHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE'>NAI</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=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'>V8H</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7ocq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ocq OCA], [https://pdbe.org/7ocq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ocq RCSB], [https://www.ebi.ac.uk/pdbsum/7ocq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ocq ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/D0C7J2_ACIB2 D0C7J2_ACIB2] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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. | ||
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| + | 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<ref>PMID:35363566</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7ocq" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Acinetobacter baumannii ATCC 19606 = CIP 70 34 = JCM 6841]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Mueller V]] | [[Category: Mueller V]] | ||
[[Category: Pos KM]] | [[Category: Pos KM]] | ||
[[Category: Tam HK]] | [[Category: Tam HK]] | ||
Current revision
NADH bound to the dehydrogenase domain of the bifunctional mannitol-1-phosphate dehydrogenase/phosphatase MtlD from Acinetobacter baumannii
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