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| | <StructureSection load='1vg3' size='340' side='right'caption='[[1vg3]], [[Resolution|resolution]] 2.70Å' scene=''> | | <StructureSection load='1vg3' size='340' side='right'caption='[[1vg3]], [[Resolution|resolution]] 2.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1vg3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43589 Atcc 43589]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VG3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1VG3 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1vg3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VG3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VG3 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1v4e|1v4e]], [[1v4h|1v4h]], [[1v4j|1v4j]], [[1v4k|1v4k]], [[1v4i|1v4i]], [[1vg2|1vg2]], [[1vg4|1vg4]], [[1vg6|1vg6]], [[1vg7|1vg7]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.84 and 2.5.1.85 2.5.1.84 and 2.5.1.85] </span></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=1vg3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vg3 OCA], [https://pdbe.org/1vg3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vg3 RCSB], [https://www.ebi.ac.uk/pdbsum/1vg3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vg3 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1vg3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vg3 OCA], [http://pdbe.org/1vg3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1vg3 RCSB], [http://www.ebi.ac.uk/pdbsum/1vg3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1vg3 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q9X1M1_THEMA Q9X1M1_THEMA] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 43589]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Transferase]] | + | [[Category: Thermotoga maritima]] |
| - | [[Category: Chou, C C]] | + | [[Category: Chou CC]] |
| - | [[Category: Guo, R T]] | + | [[Category: Guo RT]] |
| - | [[Category: Ko, T P]] | + | [[Category: Ko TP]] |
| - | [[Category: Kuo, C J]] | + | [[Category: Kuo CJ]] |
| - | [[Category: Liang, P H]] | + | [[Category: Liang PH]] |
| - | [[Category: Wang, A H.J]] | + | [[Category: Wang AH-J]] |
| - | [[Category: Thermophilic]]
| + | |
| - | [[Category: Trans-type prenyltransferase]]
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| Structural highlights
Function
Q9X1M1_THEMA
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Octaprenyl pyrophosphate synthase (OPPs) catalyzes consecutive condensation reactions of farnesyl pyrophosphate (FPP) with five molecules of isopentenyl pyrophosphate (IPP) to generate C(40) octaprenyl pyrophosphate (OPP) which constitutes the side chain of menaquinone. We have previously reported the X-ray structure of OPPs from Thermotoga maritima, which is composed entirely of alpha-helices joined by connecting loops and is arranged with nine core helices around a large central cavity [Guo, R. T., Kuo, C. J., Ko, T. P., Chou, C. C., Shr, R. L., Liang, P. H., and Wang, A. H.-J. (2004) J. Biol. Chem. 279, 4903-4912]. A76 and S77 are located on top of the active site close to where FPP is bound. A76Y and A76Y/S77F OPPs mutants produce C(20), indicating that the substituted larger residues interfere with the substrate chain elongation. Surprisingly, the A76Y/S77F mutant synthesizes a larger amount of C(20) than the A76Y mutant. In the crystal structure of the A76Y/S77F mutant, F77 is pushed away by Y76, thereby creating more space between those two large amino acids to accommodate the C(20) product. A large F132 residue at the bottom of the tunnel-shaped active site serves as the "floor" and determines the final product chain length. The substitution of F132 with a small Ala, thereby removing the blockade, led to the synthesis of a C(50) product larger than that produced by the wild-type enzyme. On the basis of the structure, we have sequentially mutated the large amino acids, including F132, L128, I123, and D62, to Ala underneath the tunnel. The products of the F132A/L128A/I123A/D62A mutant reach C(95), beyond the largest chain length generated by all known trans-prenyltransferases. Further modifications of the enzyme reaction conditions, including new IPP derivatives, may allow the preparation of high-molecular weight polyprenyl products resembling the rubber molecule.
A molecular ruler for chain elongation catalyzed by octaprenyl pyrophosphate synthase and its structure-based engineering to produce unprecedented long chain trans-prenyl products.,Guo RT, Kuo CJ, Ko TP, Chou CC, Liang PH, Wang AH Biochemistry. 2004 Jun 22;43(24):7678-86. PMID:15196010[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Guo RT, Kuo CJ, Ko TP, Chou CC, Liang PH, Wang AH. A molecular ruler for chain elongation catalyzed by octaprenyl pyrophosphate synthase and its structure-based engineering to produce unprecedented long chain trans-prenyl products. Biochemistry. 2004 Jun 22;43(24):7678-86. PMID:15196010 doi:10.1021/bi036336d
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