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| | <StructureSection load='4xpk' size='340' side='right'caption='[[4xpk]], [[Resolution|resolution]] 1.95Å' scene=''> | | <StructureSection load='4xpk' size='340' side='right'caption='[[4xpk]], [[Resolution|resolution]] 1.95Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4xpk]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XPK FirstGlance]. <br> | + | <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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4xpl|4xpl]]</td></tr> | + | </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> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">A911_06385 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1201032 Campylobacter jejuni subsp. jejuni PT14])</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=4xpk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xpk OCA], [http://pdbe.org/4xpk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xpk RCSB], [http://www.ebi.ac.uk/pdbsum/4xpk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4xpk ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A0J9X276_CAMJU A0A0J9X276_CAMJU] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Campylobacter jejuni subsp. jejuni pt14]] | + | [[Category: Campylobacter jejuni subsp. jejuni PT14]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Nam, M S]] | + | [[Category: Nam MS]] |
| - | [[Category: Namgung, B]] | + | [[Category: Namgung B]] |
| - | [[Category: Song, W S]] | + | [[Category: Song WS]] |
| - | [[Category: Yoon, S I]] | + | [[Category: Yoon SI]] |
| - | [[Category: Bacterial glycosylation]]
| + | |
| - | [[Category: Campylobacter jejuni]]
| + | |
| - | [[Category: N-acetyltransferase]]
| + | |
| - | [[Category: Pseh]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
A0A0J9X276_CAMJU
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Song WS, Nam MS, Namgung B, Yoon SI. Structural analysis of PseH, the Campylobacter jejuni N-acetyltransferase involved in bacterial O-linked glycosylation. 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 doi:http://dx.doi.org/10.1016/j.bbrc.2015.02.041
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