View source for 5xk7


==Crystal structure of Isosesquilavandulyl Diphosphate Synthase from Streptomyces sp. strain CNH-189 in complex with DMAPP==
<StructureSection load='5xk7' size='340' side='right'caption='[[5xk7]], [[Resolution|resolution]] 1.91&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5xk7]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_sp._CNH189 Streptomyces sp. CNH189]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XK7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XK7 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]] 1.911&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DMA:DIMETHYLALLYL+DIPHOSPHATE'>DMA</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=POP:PYROPHOSPHATE+2-'>POP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=5xk7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xk7 OCA], [https://pdbe.org/5xk7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xk7 RCSB], [https://www.ebi.ac.uk/pdbsum/5xk7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xk7 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/M4T4U9_9ACTN M4T4U9_9ACTN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
We report the first X-ray crystallographic structure of the "head-to-middle" prenyltransferase, isosesquilavandulyl diphosphate synthase, involved in biosynthesis of the merochlorin class of antibiotics. The protein adopts the zeta or cis-prenyl transferase fold but remarkably, unlike tuberculosinol adenosine synthase and other cis-prenyl transferases (e.g. cis-farnesyl, decaprenyl, undecaprenyl diphosphate synthases), the large, hydrophobic side chain does not occupy a central hydrophobic tunnel. Instead, it occupies a surface pocket oriented at 90 degrees to the hydrophobic tunnel. Product chain-length control is achieved by squeezing out the ligand from the conventional allylic S1 binding site, with proton abstraction being achieved using a diphosphate-Asn-Ser relay. The structures revise and unify our thinking as to the mechanism of action of many other prenyl transferases and may also be of use in engineering new merochlorin-class antibiotics.

"Head-to-Middle" and "Head-to-Tail" cis-Prenyl Transferases: Structure of Isosesquilavandulyl Diphosphate Synthase.,Gao J, Ko TP, Chen L, Malwal SR, Zhang J, Hu X, Qu F, Liu W, Huang JW, Cheng YS, Chen CC, Yang Y, Zhang Y, Oldfield E, Guo RT Angew Chem Int Ed Engl. 2018 Jan 15;57(3):683-687. doi: 10.1002/anie.201710185., Epub 2017 Dec 21. PMID:29215779<ref>PMID:29215779</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5xk7" style="background-color:#fffaf0;"></div>

==See Also==
*[[Undecaprenyl pyrophosphate synthase|Undecaprenyl pyrophosphate synthase]]
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Streptomyces sp. CNH189]]
[[Category: Chen CC]]
[[Category: Gao J]]
[[Category: Guo RT]]
[[Category: Ko TP]]
[[Category: Liu W]]