3wjk

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(New page: '''Unreleased structure''' The entry 3wjk is ON HOLD Authors: Han, X., Chen, C. C., Kuo, C. J., Huang, C. H, Zheng Y., Ko, T. P, Zhu, Z., Feng, X., Oldfield, E., Liang, P.H., Guo, R.T.,...)
Current revision (13:12, 8 November 2023) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 3wjk is ON HOLD
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==Crystal structure of Octaprenyl Pyrophosphate synthase from Escherichia coli==
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<StructureSection load='3wjk' size='340' side='right'caption='[[3wjk]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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<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>
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</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>
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<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>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors: Han, X., Chen, C. C., Kuo, C. J., Huang, C. H, Zheng Y., Ko, T. P, Zhu, Z., Feng, X., Oldfield, E., Liang, P.H., Guo, R.T., Ma, Y, H.
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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>
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Description: Crystal structure of Octaprenyl Pyrophosphate synthase from Escherichia coli
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3wjk" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Escherichia coli O104:H4 str. 2009EL-2071]]
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[[Category: Large Structures]]
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[[Category: Chen CC]]
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[[Category: Feng X]]
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[[Category: Guo RT]]
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[[Category: Han X]]
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[[Category: Huang CH]]
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[[Category: Ko TP]]
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[[Category: Kuo CJ]]
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[[Category: Liang PH]]
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[[Category: Ma YH]]
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[[Category: Oldfield E]]
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[[Category: Zheng Y]]
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[[Category: Zhu Z]]

Current revision

Crystal structure of Octaprenyl Pyrophosphate synthase from Escherichia coli

PDB ID 3wjk

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