View source for 6acs


==poly-cis-prenyltransferase==
<StructureSection load='6acs' size='340' side='right'caption='[[6acs]], [[Resolution|resolution]] 1.81&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6acs]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Acinetobacter_baumannii Acinetobacter baumannii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ACS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ACS 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]] 1.81&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</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=6acs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6acs OCA], [https://pdbe.org/6acs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6acs RCSB], [https://www.ebi.ac.uk/pdbsum/6acs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6acs ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A0D5YHU7_ACIBA A0A0D5YHU7_ACIBA] Catalyzes the sequential condensation of isopentenyl diphosphate (IPP) with (2E,6E)-farnesyl diphosphate (E,E-FPP) to yield (2Z,6Z,10Z,14Z,18Z,22Z,26Z,30Z,34E,38E)-undecaprenyl diphosphate (di-trans,octa-cis-UPP). UPP is the precursor of glycosyl carrier lipid in the biosynthesis of bacterial cell wall polysaccharide components such as peptidoglycan and lipopolysaccharide.[HAMAP-Rule:MF_01139]
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== Publication Abstract from PubMed ==
Undecaprenyl pyrophosphate (UPP) is an important carrier of the oligosaccharide component in peptidoglycan synthesis. Inhibition of UPP synthase (UPPS) may be an effective strategy in combating the pathogen Acinetobacter baumannii, which has evolved to be multidrug-resistant. Here, A. baumannii UPPS (AbUPPS) was cloned, expressed, purified and crystallized, and its structure was determined by X-ray diffraction. Each chain of the dimeric protein folds into a central beta-sheet with several surrounding alpha-helices, including one at the C-terminus. In the active site, two molecules of citrate interact with the side chains of the catalytic aspartate and serine. These observations may provide a structural basis for inhibitor design against AbUPPS.

Structure of undecaprenyl pyrophosphate synthase from Acinetobacter baumannii.,Ko TP, Huang CH, Lai SJ, Chen Y Acta Crystallogr F Struct Biol Commun. 2018 Dec 1;74(Pt 12):765-769. doi:, 10.1107/S2053230X18012931. Epub 2018 Nov 16. PMID:30511669<ref>PMID:30511669</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6acs" style="background-color:#fffaf0;"></div>

==See Also==
*[[Undecaprenyl pyrophosphate synthase|Undecaprenyl pyrophosphate synthase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Acinetobacter baumannii]]
[[Category: Large Structures]]
[[Category: Chen Y]]
[[Category: Ko T-P]]