3wjn
From Proteopedia
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| - | ''' | + | ==Crystal structure of Octaprenyl Pyrophosphate synthase from Escherichia coli with farnesyl S-thiol-pyrophosphate (FSPP)== |
| + | <StructureSection load='3wjn' size='340' side='right' caption='[[3wjn]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3wjn]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WJN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WJN FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FPS:S-[(2E,6E)-3,7,11-TRIMETHYLDODECA-2,6,10-TRIENYL]+TRIHYDROGEN+THIODIPHOSPHATE'>FPS</scene><br> | ||
| + | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3wjk|3wjk]], [[3wjo|3wjo]]</td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3wjn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wjn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wjn RCSB], [http://www.ebi.ac.uk/pdbsum/3wjn PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Chen, C C.]] | ||
| + | [[Category: Feng, X.]] | ||
| + | [[Category: Guo, R T.]] | ||
| + | [[Category: Han, X.]] | ||
| + | [[Category: Huang, C H.]] | ||
| + | [[Category: Ko, T P.]] | ||
| + | [[Category: Kuo, C J.]] | ||
| + | [[Category: Liang, P H.]] | ||
| + | [[Category: Ma, Y H.]] | ||
| + | [[Category: Oldfield, E.]] | ||
| + | [[Category: Zheng, Y.]] | ||
| + | [[Category: Zhu, Z.]] | ||
| + | [[Category: Prenyltransferase]] | ||
| + | [[Category: Product chain length]] | ||
| + | [[Category: Site-directed mutagenesis]] | ||
| + | [[Category: Transferase]] | ||
Revision as of 07:55, 18 June 2014
Crystal structure of Octaprenyl Pyrophosphate synthase from Escherichia coli with farnesyl S-thiol-pyrophosphate (FSPP)
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