4d48
From Proteopedia
(Difference between revisions)
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- | ==Crystal Structure of glucose-1-phosphate uridylyltransferase GalU from Erwinia amylovora== | + | |
+ | ==Crystal Structure of glucose-1-phosphate uridylyltransferase GalU from Erwinia amylovora.== | ||
<StructureSection load='4d48' size='340' side='right' caption='[[4d48]], [[Resolution|resolution]] 2.46Å' scene=''> | <StructureSection load='4d48' size='340' side='right' caption='[[4d48]], [[Resolution|resolution]] 2.46Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[4d48]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D48 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4D48 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4d48]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Erwac Erwac]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D48 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4D48 FirstGlance]. <br> |
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4d47|4d47]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4d47|4d47]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/UTP--glucose-1-phosphate_uridylyltransferase UTP--glucose-1-phosphate uridylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.9 2.7.7.9] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/UTP--glucose-1-phosphate_uridylyltransferase UTP--glucose-1-phosphate uridylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.9 2.7.7.9] </span></td></tr> | ||
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4d48 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d48 OCA], [http://pdbe.org/4d48 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4d48 RCSB], [http://www.ebi.ac.uk/pdbsum/4d48 PDBsum]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4d48 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d48 OCA], [http://pdbe.org/4d48 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4d48 RCSB], [http://www.ebi.ac.uk/pdbsum/4d48 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4d48 ProSAT]</span></td></tr> |
</table> | </table> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Erwinia amylovora, a Gram-negative plant pathogen, is the causal agent of Fire Blight, a contagious necrotic disease affecting plants belonging to the Rosaceae family, including apple and pear. E. amylovora is highly virulent and capable of rapid dissemination in orchards; effective control methods are still lacking. One of its most important pathogenicity factors is the exopolysaccharide amylovoran. Amylovoran is a branched polymer made by the repetition of units mainly composed of galactose, with some residues of glucose, glucuronic acid and pyruvate. E. amylovora glucose-1-phosphate uridylyltransferase (UDP-glucose pyrophosphorylase, EC 2.7.7.9) has a key role in amylovoran biosynthesis. This enzyme catalyses the production of UDP-glucose from glucose-1-phosphate and UTP, which the epimerase GalE converts into UDP-galactose, the main building block of amylovoran. We determined EaGalU kinetic parameters and substrate specificity with a range of sugar 1-phosphates. At time point 120min the enzyme catalysed conversion of the sugar 1-phosphate into the corresponding UDP-sugar reached 74% for N-acetyl-alpha-d-glucosamine 1-phosphate, 28% for alpha-d-galactose 1-phosphate, 0% for alpha-d-galactosamine 1-phosphate, 100% for alpha-d-xylose 1-phosphate, 100% for alpha-d-glucosamine 1-phosphate, 70% for alpha-d-mannose 1-phosphate, and 0% for alpha-d-galacturonic acid 1-phosphate. To explain our results we obtained the crystal structure of EaGalU and augmented our study by docking the different sugar 1-phosphates into EaGalU active site, providing both reliable models for substrate binding and enzyme specificity, and a rationale that explains the different activity of EaGalU on the sugar 1-phosphates used. These data demonstrate EaGalU potential as a biocatalyst for biotechnological purposes, as an alternative to the enzyme from Escherichia coli, besides playing an important role in E. amylovora pathogenicity. | ||
+ | |||
+ | Glucose-1-phosphate uridylyltransferase from Erwinia amylovora: Activity, structure and substrate specificity.,Benini S, Toccafondi M, Rejzek M, Musiani F, Wagstaff BA, Wuerges J, Cianci M, Field RA Biochim Biophys Acta. 2017 Nov;1865(11 Pt A):1348-1357. doi:, 10.1016/j.bbapap.2017.08.015. Epub 2017 Aug 24. PMID:28844747<ref>PMID:28844747</ref> | ||
+ | |||
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | <div class="pdbe-citations 4d48" style="background-color:#fffaf0;"></div> | ||
+ | == References == | ||
+ | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
+ | [[Category: Erwac]] | ||
[[Category: UTP--glucose-1-phosphate uridylyltransferase]] | [[Category: UTP--glucose-1-phosphate uridylyltransferase]] | ||
[[Category: Benini, S]] | [[Category: Benini, S]] |
Revision as of 06:46, 14 March 2018
Crystal Structure of glucose-1-phosphate uridylyltransferase GalU from Erwinia amylovora.
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