4m9c: Difference between revisions
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==WeeI from Acinetobacter baumannii AYE== | |||
=== | <StructureSection load='4m9c' size='340' side='right' caption='[[4m9c]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4m9c]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Aciba Aciba]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4M9C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4M9C FirstGlance]. <br> | |||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4m99|4m99]], [[4m98|4m98]]</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=4m9c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m9c OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4m9c RCSB], [http://www.ebi.ac.uk/pdbsum/4m9c PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
UDP-N,N'-diacetylbacillosamine (UDP-diNAcBac) is a unique carbohydrate produced by a number of bacterial species and has been implicated in pathogenesis. The terminal step in the formation of this important bacterial sugar is catalyzed by an AcCoA-dependent acetyltransferase in both N- and O-linked protein glycosylation pathways. This bacterial acetyltransferase is a member of the left-handed beta-helix family and forms a homotrimer as the functional unit. While previous endeavors have focused on the Campylobacter jejuni acetyltransferase (PglD) from the N-linked glycosylation pathway, structural characterization of the homologous enzymes in the O-linked glycosylation pathways is lacking. Herein, we present the apo crystal structures of the acetyltransferase domain (ATD) from the bifunctional enzyme PglB (Neisseria gonorrhoeae) and the full-length acetyltransferase WeeI (Acinetobacter baumannii). Additionally, a PglB-ATD structure was solved in complex with AcCoA. Surprisingly, this structure reveals a contrasting binding mechanism for this substrate when compared to the AcCoA-bound PglD structure. A comparison between these findings with the previously solved PglD crystal structures illustrates a dichotomy among N- and O-linked glycosylation pathway enzymes. Based upon these structures, key residues in the UDP-4-amino and AcCoA binding pockets were mutated to determine their effect on binding and catalysis in PglD, PglB-ATD, and WeeI. Lastly, a phylogenetic analysis of the aforementioned acetyltransferases was employed to illuminate the diversity among N- and O-linked glycosylation pathway enzymes. | |||
Biochemical analysis and structure determination of bacterial acetyltransferases responsible for the biosynthesis of UDP-N,N'-diacetylbacillosamine.,Morrison MJ, Imperiali B J Biol Chem. 2013 Sep 24. PMID:24064219<ref>PMID:24064219</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Aciba]] | [[Category: Aciba]] | ||
[[Category: Imperiali, B.]] | [[Category: Imperiali, B.]] | ||
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[[Category: Acetyltransferase]] | [[Category: Acetyltransferase]] | ||
[[Category: Left-handed beta-helix]] | [[Category: Left-handed beta-helix]] | ||
[[Category: | [[Category: Rossmann fold]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
Revision as of 14:26, 3 November 2014
WeeI from Acinetobacter baumannii AYE
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