View source for 22ao


==Crystal structure of Bacillus cereus GmaR in the apo form==
<StructureSection load='22ao' size='340' side='right'caption='[[22ao]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[22ao]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_cereus Bacillus cereus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=22AO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=22AO 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]] 2.8&#8491;</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=22ao FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=22ao OCA], [https://pdbe.org/22ao PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=22ao RCSB], [https://www.ebi.ac.uk/pdbsum/22ao PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=22ao ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
GmaR was identified in Listeria monocytogenes as an essential dual-function protein that regulates the MogR-mediated repression of flagellar gene expression and catalyzes the glycosylation of the flagellar protein flagellin. To elucidate the structural and molecular basis of GmaR function, we determined the crystal structure of Bacillus cereus GmaR (bcGmaR) and investigated its glycosyltransferase and regulatory activities through structure-based biochemical and mutational analyses. Unexpectedly, bcGmaR does not interact with MogR and is unlikely to function as a MogR regulator in contrast to L. monocytogenes GmaR. Instead, bcGmaR catalyzes Mg(2+)-dependent O-linked N-acetylglucosamine (GlcNAc) transfer to B. cereus flagellin, substantially increasing its thermostability. The N-terminal glycosyltransferase (GT) domain of bcGmaR adopts a three-layer GT-A type fold with a pocket, which accommodates Mg(2+) and the sugar donor UDP-GlcNAc through the canonical DxD and C-His motifs conserved among GT-A enzymes, as well as a bcGmaR-specific phiHE motif located within a unique beta-hairpin structure. Notably, the phiHE motif is critical for catalysis, potentially by providing the catalytic base. In addition to the GT domain, the tetratricopeptide repeat domain is also required for full enzymatic activity. These findings highlight the functional divergence of GmaRs among bacterial species and underscore their unique catalytic features.

Bacillus cereus GmaR glycosylates flagellin through a unique structural motif but is uncoupled from MogR regulation.,Oh HB, Lee SJ, Yoon SI Int J Biol Macromol. 2026 May;360:151808. doi: 10.1016/j.ijbiomac.2026.151808. , Epub 2026 Apr 3. PMID:41937015<ref>PMID:41937015</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 22ao" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bacillus cereus]]
[[Category: Large Structures]]
[[Category: Lee SJ]]
[[Category: Oh HB]]
[[Category: Yoon SI]]