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==Crystal structure of Octaprenyl Pyrophosphate synthase from Escherichia coli==
<StructureSection load='3wjk' size='340' side='right'caption='[[3wjk]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3wjk]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_O104:H4_str._2009EL-2071 Escherichia coli O104:H4 str. 2009EL-2071]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WJK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WJK 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]] 2.2&#8491;</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=3wjk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wjk OCA], [https://pdbe.org/3wjk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wjk RCSB], [https://www.ebi.ac.uk/pdbsum/3wjk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wjk ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
Octaprenyl pyrophosphate synthase (OPPs) catalyzes consecutive condensation reactions of one allylic substrate farnesyl pyrophosphate (FPP) and five homoallylic substrate isopentenyl pyrophosphate (IPP) molecules to form a C40 long-chain product OPP, which serves as a side chain of ubiquinone and menaquinone. OPPs belongs to the trans-prenyltransferase class of proteins. The structures of OPPs from Escherichia coli were solved in the apo-form as well as in complexes with IPP and a FPP thio-analog, FsPP, at resolutions of 2.2 to 2.6 A, and revealed the detailed interactions between the ligands and enzyme. At the bottom of the active-site tunnel, M123 and M135 act in concert to form a wall which determines the final chain length. These results represent the first ligand-bound crystal structures of a long-chain trans-prenyltransferase and provide new information on the mechanisms of catalysis and product chain elongation. (c) Proteins 2014;. (c) 2014 Wiley Periodicals, Inc.

Crystal structures of ligand-bound octaprenyl pyrophosphate synthase from escherichia coli reveal the catalytic and chain-length determining mechanisms.,Han X, Chen CC, Kuo CJ, Huang CH, Zheng Y, Ko TP, Zhu Z, Feng X, Wang K, Oldfield E, Wang AH, Liang PH, Guo RT, Ma Y Proteins. 2014 Jun 4. doi: 10.1002/prot.24618. PMID:24895191<ref>PMID:24895191</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli O104:H4 str. 2009EL-2071]]
[[Category: Large Structures]]
[[Category: Chen CC]]
[[Category: Feng X]]
[[Category: Guo RT]]
[[Category: Han X]]
[[Category: Huang CH]]
[[Category: Ko TP]]
[[Category: Kuo CJ]]
[[Category: Liang PH]]
[[Category: Ma YH]]
[[Category: Oldfield E]]
[[Category: Zheng Y]]
[[Category: Zhu Z]]