View source for 5tyh


==PglD from Campylobacter jejuni NCTC 11168 in complex with 5-(2-furanyl)-1H-pyrazole-3-carboxylic acid==
<StructureSection load='5tyh' size='340' side='right'caption='[[5tyh]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5tyh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Campylobacter_jejuni_subsp._jejuni_NCTC_11168_=_ATCC_700819 Campylobacter jejuni subsp. jejuni NCTC 11168 = ATCC 700819]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TYH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5TYH 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]] 2.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=7O4:3-(FURAN-2-YL)-1H-PYRAZOLE-5-CARBOXYLIC+ACID'>7O4</scene></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=5tyh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tyh OCA], [https://pdbe.org/5tyh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5tyh RCSB], [https://www.ebi.ac.uk/pdbsum/5tyh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5tyh ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PGLD_CAMJE PGLD_CAMJE] Acetyltransferase that modifies the UDP-4-amino-sugar to form UDP-N,N'-diacetylbacillosamine in the N-linked protein glycosylation pathway.<ref>PMID:17087520</ref> <ref>PMID:19448740</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The glycoproteins of selected microbial pathogens often include highly modified carbohydrates such as 2,4-diacetamidobacillosamine (diNAcBac). These glycoconjugates are involved in host-cell interactions and may be associated with the virulence of medically significant Gram-negative bacteria. In light of genetic studies demonstrating the attenuated virulence of bacterial strains in which modified carbohydrate biosynthesis enzymes have been knocked out, we are developing small molecule inhibitors of selected enzymes as tools to evaluate whether such compounds modulate virulence. We performed fragment-based and high-throughput screens against an amino-sugar acetyltransferase enzyme, PglD, involved in biosynthesis of UDP-diNAcBac in Campylobacter jejuni. Herein we report optimization of the hits into potent small molecule inhibitors (IC50 &lt; 300 nM). Biophysical characterization shows that the best inhibitors are competitive with acetyl coenzyme A and an X-ray cocrystal structure reveals that binding is biased toward occupation of the adenine subpocket of the AcCoA binding site by an aromatic ring.

Targeting Bacillosamine Biosynthesis in Bacterial Pathogens: Development of Inhibitors to a Bacterial Amino-Sugar Acetyltransferase from Campylobacter jejuni.,De Schutter JW, Morrison JP, Morrison MJ, Ciulli A, Imperiali B J Med Chem. 2017 Feb 22. doi: 10.1021/acs.jmedchem.6b01869. PMID:28182413<ref>PMID:28182413</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5tyh" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Campylobacter jejuni subsp. jejuni NCTC 11168 = ATCC 700819]]
[[Category: Large Structures]]
[[Category: Imperiali B]]
[[Category: Morrison JP]]