View source for 4xpk


==The crystal structure of Campylobacter jejuni N-acetyltransferase PseH==
<StructureSection load='4xpk' size='340' side='right'caption='[[4xpk]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4xpk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Campylobacter_jejuni_subsp._jejuni_PT14 Campylobacter jejuni subsp. jejuni PT14]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XPK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XPK 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]] 1.95&#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=4xpk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xpk OCA], [https://pdbe.org/4xpk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xpk RCSB], [https://www.ebi.ac.uk/pdbsum/4xpk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xpk ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A0J9X276_CAMJU A0A0J9X276_CAMJU] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Campylobacter jejuni is a bacterium that uses flagella for motility and causes worldwide acute gastroenteritis in humans. The C. jejuni N-acetyltransferase PseH (cjPseH) is responsible for the third step in flagellin O-linked glycosylation and plays a key role in flagellar formation and motility. cjPseH transfers an acetyl group from an acetyl donor, acetyl coenzyme A (AcCoA), to the amino group of UDP-4-amino-4,6-dideoxy-N-acetyl-beta-l-altrosamine to produce UDP-2,4-diacetamido-2,4,6-trideoxy-beta-l-altropyranose. To elucidate the catalytic mechanism of cjPseH, crystal structures of cjPseH alone and in complex with AcCoA were determined at 1.95 A resolution. cjPseH folds into a single-domain structure of a central beta-sheet decorated by four alpha-helices with two continuously connected grooves. A deep groove (groove-A) accommodates the AcCoA molecule. Interestingly, the acetyl end of AcCoA points toward an open space in a neighboring shallow groove (groove-S), which is occupied by extra electron density that potentially serves as a pseudosubstrate, suggesting that the groove-S may provide a substrate-binding site. Structure-based comparative analysis suggests that cjPseH utilizes a unique catalytic mechanism of acetylation that has not been observed in other glycosylation-associated acetyltransferases. Thus, our studies on cjPseH will provide valuable information for the design of new antibiotics to treat C. jejuni-induced gastroenteritis.

Structural analysis of PseH, the Campylobacter jejuni N-acetyltransferase involved in bacterial O-linked glycosylation.,Song WS, Nam MS, Namgung B, Yoon SI Biochem Biophys Res Commun. 2015 Mar 20;458(4):843-8. doi:, 10.1016/j.bbrc.2015.02.041. Epub 2015 Feb 16. PMID:25698400<ref>PMID:25698400</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4xpk" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Campylobacter jejuni subsp. jejuni PT14]]
[[Category: Large Structures]]
[[Category: Nam MS]]
[[Category: Namgung B]]
[[Category: Song WS]]
[[Category: Yoon SI]]