7bbz
From Proteopedia
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==Crystal structure of apo aldo-keto reductase from Agrobacterium tumefaciens== | ==Crystal structure of apo aldo-keto reductase from Agrobacterium tumefaciens== | ||
- | <StructureSection load='7bbz' size='340' side='right'caption='[[7bbz]]' scene=''> | + | <StructureSection load='7bbz' size='340' side='right'caption='[[7bbz]], [[Resolution|resolution]] 1.77Å' 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=7BBZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7BBZ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7bbz]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Agrobacterium_fabrum_str._C58 Agrobacterium fabrum str. C58]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7BBZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7BBZ 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=7bbz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7bbz OCA], [https://pdbe.org/7bbz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7bbz RCSB], [https://www.ebi.ac.uk/pdbsum/7bbz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7bbz 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]] 1.77Å</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=7bbz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7bbz OCA], [https://pdbe.org/7bbz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7bbz RCSB], [https://www.ebi.ac.uk/pdbsum/7bbz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7bbz ProSAT]</span></td></tr> | ||
</table> | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/A9CEY6_AGRFC A9CEY6_AGRFC] | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Catabolism of sulfoquinovose (SQ; 6-deoxy-6-sulfoglucose), the ubiquitous sulfosugar produced by photosynthetic organisms, is an important component of the biogeochemical carbon and sulfur cycles. Here, we describe a pathway for SQ degradation that involves oxidative desulfurization to release sulfite and enable utilization of the entire carbon skeleton of the sugar to support the growth of the plant pathogen Agrobacterium tumefaciens SQ or its glycoside sulfoquinovosyl glycerol are imported into the cell by an ATP-binding cassette transporter system with an associated SQ binding protein. A sulfoquinovosidase hydrolyzes the SQ glycoside and the liberated SQ is acted on by a flavin mononucleotide-dependent sulfoquinovose monooxygenase, in concert with an NADH-dependent flavin reductase, to release sulfite and 6-oxo-glucose. An NAD(P)H-dependent oxidoreductase reduces the 6-oxo-glucose to glucose, enabling entry into primary metabolic pathways. Structural and biochemical studies provide detailed insights into the recognition of key metabolites by proteins in this pathway. Bioinformatic analyses reveal that the sulfoquinovose monooxygenase pathway is distributed across Alpha- and Betaproteobacteria and is especially prevalent within the Rhizobiales order. This strategy for SQ catabolism is distinct from previously described pathways because it enables the complete utilization of all carbons within SQ by a single organism with concomitant production of inorganic sulfite. | ||
+ | |||
+ | Oxidative desulfurization pathway for complete catabolism of sulfoquinovose by bacteria.,Sharma M, Lingford JP, Petricevic M, Snow AJD, Zhang Y, Jarva MA, Mui JW, Scott NE, Saunders EC, Mao R, Epa R, da Silva BM, Pires DEV, Ascher DB, McConville MJ, Davies GJ, Williams SJ, Goddard-Borger ED Proc Natl Acad Sci U S A. 2022 Jan 25;119(4). pii: 2116022119. doi:, 10.1073/pnas.2116022119. PMID:35074914<ref>PMID:35074914</ref> | ||
+ | |||
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | <div class="pdbe-citations 7bbz" style="background-color:#fffaf0;"></div> | ||
+ | == References == | ||
+ | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
+ | [[Category: Agrobacterium fabrum str. C58]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Davies GJ]] | [[Category: Davies GJ]] | ||
[[Category: Sharma M]] | [[Category: Sharma M]] | ||
[[Category: Snow A]] | [[Category: Snow A]] |
Current revision
Crystal structure of apo aldo-keto reductase from Agrobacterium tumefaciens
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