View source for 5jo9


==Structural characterization of the thermostable Bradyrhizobium japonicum d-sorbitol dehydrogenase==
<StructureSection load='5jo9' size='340' side='right'caption='[[5jo9]], [[Resolution|resolution]] 2.89&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5jo9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bradyrhizobium_japonicum Bradyrhizobium japonicum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JO9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JO9 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.894&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SOR:D-SORBITOL'>SOR</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=5jo9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jo9 OCA], [https://pdbe.org/5jo9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jo9 RCSB], [https://www.ebi.ac.uk/pdbsum/5jo9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jo9 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q89FN7_BRADU Q89FN7_BRADU] 
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== Publication Abstract from PubMed ==
Bradyrhizobium japonicum sorbitol dehydrogenase is NADH-dependent and is active at elevated temperatures. The best substrate is D-glucitol (a synonym for D-sorbitol), although L-glucitol is also accepted, giving it particular potential in industrial applications. Crystallization led to a hexagonal crystal form, with crystals diffracting to 2.9 A resolution. In attempts to phase the data, a molecular-replacement solution based upon PDB entry 4nbu (33% identical in sequence to the target) was found. The solution contained one molecule in the asymmetric unit, but a tetramer similar to that found in other short-chain dehydrogenases, including the search model, could be reconstructed by applying crystallographic symmetry operations. The active site contains electron density consistent with D-glucitol and phosphate, but there was not clear evidence for the binding of NADH. In a search for the features that determine the thermostability of the enzyme, the Tm for the orthologue from Rhodobacter sphaeroides, for which the structure was already known, was also determined, and this enzyme proved to be considerably less thermostable. A continuous beta-sheet is formed between two monomers in the tetramer of the B. japonicum enzyme, a feature not generally shared by short-chain dehydrogenases, and which may contribute to thermostability, as may an increased Pro/Gly ratio.

Structural characterization of the thermostable Bradyrhizobium japonicumD-sorbitol dehydrogenase.,Fredslund F, Otten H, Gemperlein S, Poulsen JC, Carius Y, Kohring GW, Lo Leggio L Acta Crystallogr F Struct Biol Commun. 2016 Nov 1;72(Pt 11):846-852. doi:, 10.1107/S2053230X16016927. Epub 2016 Oct 27. PMID:27827356<ref>PMID:27827356</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 5jo9" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bradyrhizobium japonicum]]
[[Category: Large Structures]]
[[Category: Fredslund F]]
[[Category: Lo Leggio L]]
[[Category: Navarro Poulsen J-C]]
[[Category: Otten H]]