6aav
From Proteopedia
(Difference between revisions)
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<StructureSection load='6aav' size='340' side='right'caption='[[6aav]], [[Resolution|resolution]] 1.72Å' scene=''> | <StructureSection load='6aav' size='340' side='right'caption='[[6aav]], [[Resolution|resolution]] 1.72Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6aav]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AAV OCA]. For a <b>guided tour on the structure components</b> use [http:// | + | <table><tr><td colspan='2'>[[6aav]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_campestris"_pammel_1895 "bacillus campestris" pammel 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AAV OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6AAV FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">xgtA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=339 "Bacillus campestris" Pammel 1895])</td></tr> |
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6aav FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6aav OCA], [http://pdbe.org/6aav PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6aav RCSB], [http://www.ebi.ac.uk/pdbsum/6aav PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6aav ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The alpha-glucosyl transfer enzyme XgtA is a novel type alpha-Glucosidase (EC 3.2.1.20) produced by Xanthomonas campestris WU-9701. One of the unique properties of XgtA is that it shows extremely high alpha-glucosylation activity toward alcoholic and phenolic -OH groups in compounds using maltose as an alpha-glucosyl donor and allows for the synthesis of various useful alpha-glucosides with high yields. XgtA shows no hydrolytic activity toward sucrose and no alpha-glucosylation activity toward saccharides to produce oligosaccharides. In this report, the crystal structure of XgtA was solved at 1.72 A resolution. The crystal belonged to space group P22121, with unit-cell parameters a = 73.07, b = 83.48, and c = 180.79 A. The beta-->alpha loop 4 of XgtA, which is proximal to the catalytic center, formed a unique structure that is not observed in XgtA homologs. Furthermore, XgtA was found to contain unique amino acid residues around its catalytic center. The unique structure of XgtA provides an insight into the mechanism for the regulation of substrate specificity in this enzyme. | ||
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| + | Crystal structure of alpha-glucosyl transfer enzyme XgtA from Xanthomonas campestris WU-9701.,Watanabe R, Arimura Y, Ishii Y, Kirimura K Biochem Biophys Res Commun. 2020 Jun 4;526(3):580-585. doi:, 10.1016/j.bbrc.2020.03.109. Epub 2020 Apr 1. PMID:32247611<ref>PMID:32247611</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6aav" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Bacillus campestris pammel 1895]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Arimura, Y]] | [[Category: Arimura, Y]] | ||
Revision as of 05:42, 13 May 2020
Crystal structure of alpha-glucosyl transfer enzyme, XgtA at 1.72 angstrom resolution
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