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| | <StructureSection load='2y0d' size='340' side='right'caption='[[2y0d]], [[Resolution|resolution]] 2.80Å' scene=''> | | <StructureSection load='2y0d' size='340' side='right'caption='[[2y0d]], [[Resolution|resolution]] 2.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2y0d]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/"pseudomonas_cepacia"_burkholder_1950 "pseudomonas cepacia" burkholder 1950]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Y0D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Y0D FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2y0d]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Burkholderia_cepacia Burkholderia cepacia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Y0D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Y0D FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UGA:URIDINE-5-DIPHOSPHATE-GLUCURONIC+ACID'>UGA</scene></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]] 2.8Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2y0e|2y0e]], [[2y0c|2y0c]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UGA:URIDINE-5-DIPHOSPHATE-GLUCURONIC+ACID'>UGA</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/UDP-glucose_6-dehydrogenase UDP-glucose 6-dehydrogenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.22 1.1.1.22] </span></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=2y0d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y0d OCA], [https://pdbe.org/2y0d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2y0d RCSB], [https://www.ebi.ac.uk/pdbsum/2y0d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2y0d ProSAT]</span></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=2y0d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y0d OCA], [https://pdbe.org/2y0d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2y0d RCSB], [https://www.ebi.ac.uk/pdbsum/2y0d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2y0d ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/C9E261_BURCE C9E261_BURCE] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Pseudomonas cepacia burkholder 1950]] | + | [[Category: Burkholderia cepacia]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: UDP-glucose 6-dehydrogenase]]
| + | [[Category: Borges P]] |
| - | [[Category: Borges, P]] | + | [[Category: Fialho AM]] |
| - | [[Category: Fialho, A M]] | + | [[Category: Frazao C]] |
| - | [[Category: Frazao, C]] | + | [[Category: Mil-Homens D]] |
| - | [[Category: Mil-Homens, D]] | + | [[Category: Popescu AO]] |
| - | [[Category: Popescu, A O]] | + | [[Category: Rocha J]] |
| - | [[Category: Rocha, J]] | + | [[Category: Sa-Correia I]] |
| - | [[Category: Sa-Correia, I]] | + | |
| - | [[Category: Carbohydrate synthesis]]
| + | |
| - | [[Category: Cystic fibrosis]]
| + | |
| - | [[Category: Exopolysaccharide]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
C9E261_BURCE
Publication Abstract from PubMed
Members of the Burkholderia cepacia complex (BCC) are serious respiratory pathogens in immunocompromised individuals and in patients with cystic fibrosis (CF). They are exceptionally resistant to many antimicrobial agents and have the capacity to spread between patients, leading to a decline in lung function and necrotizing pneumonia. BCC members often express a mucoid phenotype associated with the secretion of the exopolysaccharide (EPS) cepacian. There is much evidence supporting the fact that cepacian is a major virulence factor of BCC. UDP-glucose dehydrogenase (UGD) is responsible for the NAD-dependent 2-fold oxidation of UDP-glucose (UDP-Glc) to UDP-glucuronic acid (UDP-GlcA), which is a key step in cepacian biosynthesis. Here, we report the structure of BceC, determined at 1.75-A resolution. Mutagenic studies were performed on the active sites of UGDs, and together with the crystallographic structures, they elucidate the molecular mechanism of this family of sugar nucleotide-modifying enzymes. Superposition with the structures of human and other bacterial UGDs showed an active site with high structural homology. This family contains a strictly conserved tyrosine residue (Y10 in BceC; shown in italics) within the glycine-rich motif (GXGYXG) of its N-terminal Rossmann-like domain. We constructed several BceC Y10 mutants, revealing only residual dehydrogenase activity and thus highlighting the importance of this conserved residue in the catalytic activity of BceC. Based on the literature of the UGD/GMD nucleotide sugar 6-dehydrogenase family and the kinetic and structural data we obtained for BceC, we determined Y10 as a key catalytic residue in a UGD rate-determining step, the final hydrolysis of the enzymatic thioester intermediate.
Structure of Burkholderia cepacia UDP-Glucose Dehydrogenase (UGD) BceC and Role of Tyr10 in Final Hydrolysis of UGD Thioester Intermediate.,Rocha J, Popescu AO, Borges P, Mil-Homens D, Moreira LM, Sa-Correia I, Fialho AM, Frazao C J Bacteriol. 2011 Aug;193(15):3978-87. Epub 2011 May 20. PMID:21602353[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Rocha J, Popescu AO, Borges P, Mil-Homens D, Moreira LM, Sa-Correia I, Fialho AM, Frazao C. Structure of Burkholderia cepacia UDP-Glucose Dehydrogenase (UGD) BceC and Role of Tyr10 in Final Hydrolysis of UGD Thioester Intermediate. J Bacteriol. 2011 Aug;193(15):3978-87. Epub 2011 May 20. PMID:21602353 doi:10.1128/JB.01076-10
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