4xpl: Difference between revisions
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''' | ==The crystal structure of Campylobacter jejuni N-acetyltransferase PseH in complex with acetyl coenzyme A== | ||
<StructureSection load='4xpl' size='340' side='right' caption='[[4xpl]], [[Resolution|resolution]] 1.95Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4xpl]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XPL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XPL FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4xpk|4xpk]]</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4xpl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xpl OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4xpl RCSB], [http://www.ebi.ac.uk/pdbsum/4xpl PDBsum]</span></td></tr> | |||
</table> | |||
<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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
[[Category: | __TOC__ | ||
</StructureSection> | |||
[[Category: Nam, M S]] | |||
[[Category: Namgung, B]] | [[Category: Namgung, B]] | ||
[[Category: | [[Category: Song, W S]] | ||
[[Category: | [[Category: Yoon, S I]] | ||
[[Category: Bacterial glycosylation]] | |||
[[Category: Campylobacter jejuni]] | |||
[[Category: N-acetyltransferase]] | |||
[[Category: Pseh]] | |||
[[Category: Transferase]] | |||
Revision as of 12:00, 18 March 2015
The crystal structure of Campylobacter jejuni N-acetyltransferase PseH in complex with acetyl coenzyme A
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