View source for 7fe4


==Crystal structure of GH65 alpha-1,2-glucosidase from Flavobacterium johnsoniae in complex with glucose==
<StructureSection load='7fe4' size='340' side='right'caption='[[7fe4]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7fe4]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Flavobacterium_johnsoniae_UW101 Flavobacterium johnsoniae UW101]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7FE4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7FE4 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]] 1.4&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</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=7fe4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7fe4 OCA], [https://pdbe.org/7fe4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7fe4 RCSB], [https://www.ebi.ac.uk/pdbsum/7fe4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7fe4 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A5FBJ5_FLAJ1 A5FBJ5_FLAJ1] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Glycoside hydrolase family 65 (GH65) comprises glycoside hydrolases (GHs) and glycoside phosphorylases (GPs) that act on alpha-glucosidic linkages in oligosaccharides. All previously reported bacterial GH65 enzymes are GPs, whereas all eukaryotic GH65 enzymes known are GHs. In addition, to date, no crystal structure of a GH65 GH has yet been reported. In this study, we use biochemical experiments and X-ray crystallography to examine the function and structure of a GH65 enzyme from Flavobacterium johnsoniae (FjGH65A) that shows low amino acid sequence homology to reported GH65 enzymes. We found that FjGH65A does not exhibit phosphorolytic activity, but it does hydrolyze kojibiose (alpha-1,2-glucobiose) and oligosaccharides containing a kojibiosyl moiety without requiring inorganic phosphate. In addition, stereochemical analysis demonstrated that FjGH65A catalyzes this hydrolytic reaction via an anomer-inverting mechanism. The three-dimensional structures of FjGH65A in native form and in complex with glucose were determined at resolutions of 1.54 and 1.40 A resolutions, respectively. The overall structure of FjGH65A resembled those of other GH65 GPs, and the general acid catalyst Glu(472) was conserved. However, the amino acid sequence forming the phosphate-binding site typical of GH65 GPs was not conserved in FjGH65A. Moreover, FjGH65A had the general base catalyst Glu(616) instead, which is required to activate a nucleophilic water molecule. These results indicate that FjGH65A is an alpha-1,2-glucosidase and is the first bacterial GH found in the GH65 family.

Structure of a bacterial alpha-1,2-glucosidase defines mechanisms of hydrolysis and substrate specificity in GH65 family hydrolases.,Nakamura S, Nihira T, Kurata R, Nakai H, Funane K, Park EY, Miyazaki T J Biol Chem. 2021 Oct 30;297(6):101366. doi: 10.1016/j.jbc.2021.101366. PMID:34728215<ref>PMID:34728215</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7fe4" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Flavobacterium johnsoniae UW101]]
[[Category: Large Structures]]
[[Category: Miyazaki T]]
[[Category: Nakamura S]]