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7byu
From Proteopedia
(Difference between revisions)
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==Crystal structure of Acidovorax avenae L-fucose mutarotase (apo form)== | ==Crystal structure of Acidovorax avenae L-fucose mutarotase (apo form)== | ||
| - | <StructureSection load='7byu' size='340' side='right'caption='[[7byu]]' scene=''> | + | <StructureSection load='7byu' size='340' side='right'caption='[[7byu]], [[Resolution|resolution]] 2.21Å' 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=7BYU OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=7BYU FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7byu]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Aciap Aciap]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7BYU OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=7BYU FirstGlance]. <br> |
| - | </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=7byu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7byu OCA], [http://pdbe.org/7byu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=7byu RCSB], [http://www.ebi.ac.uk/pdbsum/7byu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=7byu ProSAT]</span></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1PG:2-(2-{2-[2-(2-METHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHANOL'>1PG</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr> |
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Acav_1655 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=643561 ACIAP])</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=7byu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7byu OCA], [http://pdbe.org/7byu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=7byu RCSB], [http://www.ebi.ac.uk/pdbsum/7byu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=7byu ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Mutarotases catalyze the alpha-beta anomeric conversion of monosaccharide, and play a key role in utilizing sugar as enzymes involved in sugar metabolism have specificity for the alpha- or beta-anomer. In spite of the sequential similarity to l-rhamnose mutarotase protein superfamily (COG3254: RhaM), the ACAV_RS08160 gene in Acidovorax avenae ATCC 19860 (AaFucM) is located in a gene cluster related to non-phosphorylative l-fucose and l-galactose metabolism, and transcriptionally induced by these carbon sources; therefore, the physiological role remains unclear. Here, we report that AaFucM possesses mutarotation activity only toward l-fucose by saturation difference (SD) NMR experiments. Moreover, we determined the crystal structures of AaFucM in the apo form and in the l-fucose-bound form at resolutions of 2.21 and 1.75 A, respectively. The overall structural folding was clearly similar to the RhaM members, differed from the known l-fucose mutarotase (COG4154: FucU), strongly indicating their convergent evolution. The structure-based mutational analyses suggest that Tyr18 is important for catalytic action, and that Gln87 and Trp99 are involved in the l-fucose-specific recognition. | ||
| + | |||
| + | Functional and structural characterization of a novel L-fucose mutarotase involved in non-phosphorylative pathway of L-fucose metabolism.,Watanabe Y, Watanabe S, Fukui Y, Nishiwaki H Biochem Biophys Res Commun. 2020 May 21. pii: S0006-291X(20)31015-9. doi:, 10.1016/j.bbrc.2020.05.094. PMID:32448506<ref>PMID:32448506</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7byu" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Aciap]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Fukui Y]] | + | [[Category: Fukui, Y]] |
| - | [[Category: Watanabe S]] | + | [[Category: Watanabe, S]] |
| - | [[Category: Watanabe Y]] | + | [[Category: Watanabe, Y]] |
| + | [[Category: L-fucose]] | ||
| + | [[Category: Mutarotase]] | ||
| + | [[Category: Sugar binding protein]] | ||
Revision as of 06:55, 10 June 2020
Crystal structure of Acidovorax avenae L-fucose mutarotase (apo form)
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