1wl3
From Proteopedia
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|SITE= | |SITE= | ||
|LIGAND= | |LIGAND= | ||
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Trans-octaprenyltranstransferase Trans-octaprenyltranstransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.11 2.5.1.11] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Trans-octaprenyltranstransferase Trans-octaprenyltranstransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.11 2.5.1.11] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1v4e|1V4E]], [[1v4h|1V4H]], [[1v4j|1V4J]], [[1v4k|1V4K]], [[1v4i|1V4I]], [[1wkz|1WKZ]], [[1wl0|1WL0]], [[1wl1|1WL1]], [[1wl2|1WL2]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1wl3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wl3 OCA], [http://www.ebi.ac.uk/pdbsum/1wl3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1wl3 RCSB]</span> | ||
}} | }} | ||
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[[Category: trans-type prenyltransferase]] | [[Category: trans-type prenyltransferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:37:40 2008'' |
Revision as of 21:37, 30 March 2008
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| , resolution 3.5Å | |||||||
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| Activity: | Trans-octaprenyltranstransferase, with EC number 2.5.1.11 | ||||||
| Related: | 1V4E, 1V4H, 1V4J, 1V4K, 1V4I, 1WKZ, 1WL0, 1WL1, 1WL2
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure Of Octaprenyl Pyrophosphate Synthase From Hyperthermophilic Thermotoga Maritima R91A mutant
Overview
Octaprenyl pyrophosphate synthase (OPPs) catalyzes the condensation of five isopentenyl pyrophosphates with farnesyl pyrophosphate to generate C(40) octaprenyl pyrophosphate. The enzymes from the hyperthermophilic bacterium Thermotoga maritima and from the mesophilic Escherichia coli were expressed in E. coli and the recombinant proteins were purified and crystallized. The T. maritima OPPs crystals belong to space group P42(1)2, with unit-cell parameters a = b = 151.53, c = 69.72 A. The E. coli OPPs crystals belong to space group C222(1), with unit-cell parameters a = 247.66, b = 266.10, c = 157.93 A. Diffraction data were collected at 100 K using synchrotron radiation and an in-house X-ray source. Structure determination of T. maritima OPPs has been carried out using MIR data sets at 2.8 A resolution. The asymmetric unit contains one dimer. An initial model with 280 residues per subunit has been built and refined to 2.28 A resolution. It shows mostly helical structure and resembles that of avian farnesyl pyrophosphate synthase.
About this Structure
1WL3 is a Single protein structure of sequence from Thermotoga maritima msb8. Full crystallographic information is available from OCA.
Reference
Preliminary X-ray diffraction analysis of octaprenyl pyrophosphate synthase crystals from Thermotoga maritima and Escherichia coli., Guo RT, Ko TP, Chou CC, Shr HL, Chu HM, Tsai YH, Liang PH, Wang AH, Acta Crystallogr D Biol Crystallogr. 2003 Dec;59(Pt 12):2265-8. Epub 2003, Nov 27. PMID:14646090
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