View source for 7byw


==Crystal structure of Acidovorax avenae L-fucose mutarotase (L-fucose-bound form)==
<StructureSection load='7byw' size='340' side='right'caption='[[7byw]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7byw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Acidovorax_avenae_subsp._avenae_ATCC_19860 Acidovorax avenae subsp. avenae ATCC 19860]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7BYW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7BYW FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75&#8491;</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=FUC:ALPHA-L-FUCOSE'>FUC</scene></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=7byw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7byw OCA], [https://pdbe.org/7byw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7byw RCSB], [https://www.ebi.ac.uk/pdbsum/7byw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7byw ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/F0Q4R9_ACIAP F0Q4R9_ACIAP] 
<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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7byw" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Acidovorax avenae subsp. avenae ATCC 19860]]
[[Category: Large Structures]]
[[Category: Watanabe S]]
[[Category: Watanabe Y]]