1wl0: Difference between revisions

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{{STRUCTURE_1wl0|  PDB=1wl0  |  SCENE=  }}  
{{STRUCTURE_1wl0|  PDB=1wl0  |  SCENE=  }}  


'''Crystal Structure Of Octaprenyl Pyrophosphate Synthase From Hyperthermophilic Thermotoga Maritima R44A mutant'''
===Crystal Structure Of Octaprenyl Pyrophosphate Synthase From Hyperthermophilic Thermotoga Maritima R44A 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==
==About this Structure==
1WL0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima_msb8 Thermotoga maritima msb8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WL0 OCA].  
1WL0 is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Thermotoga_maritima_msb8 Thermotoga maritima msb8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WL0 OCA].  


==Reference==
==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:[http://www.ncbi.nlm.nih.gov/pubmed/14646090 14646090]
<ref group="xtra">PMID:14646090</ref><ref group="xtra">PMID:14617622</ref><ref group="xtra">PMID:15196010</ref><references group="xtra"/>
[[Category: Single protein]]
[[Category: Thermotoga maritima msb8]]
[[Category: Thermotoga maritima msb8]]
[[Category: Trans-octaprenyltranstransferase]]
[[Category: Trans-octaprenyltranstransferase]]
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[[Category: Thermophilic]]
[[Category: Thermophilic]]
[[Category: Trans-type prenyltransferase]]
[[Category: Trans-type prenyltransferase]]
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Revision as of 19:31, 16 February 2009

File:1wl0.png

Template:STRUCTURE 1wl0

Crystal Structure Of Octaprenyl Pyrophosphate Synthase From Hyperthermophilic Thermotoga Maritima R44A mutantCrystal Structure Of Octaprenyl Pyrophosphate Synthase From Hyperthermophilic Thermotoga Maritima R44A mutant

About this StructureAbout this Structure

1WL0 is a 2 chains structure of sequences from Thermotoga maritima msb8. Full crystallographic information is available from OCA.

ReferenceReference

[xtra 1][xtra 2][xtra 3]

  1. Guo RT, Ko TP, Chou CC, Shr HL, Chu HM, Tsai YH, Liang PH, Wang AH. Preliminary X-ray diffraction analysis of octaprenyl pyrophosphate synthase crystals from Thermotoga maritima and Escherichia coli. Acta Crystallogr D Biol Crystallogr. 2003 Dec;59(Pt 12):2265-8. Epub 2003, Nov 27. PMID:14646090
  2. Guo RT, Kuo CJ, Chou CC, Ko TP, Shr HL, Liang PH, Wang AH. Crystal structure of octaprenyl pyrophosphate synthase from hyperthermophilic Thermotoga maritima and mechanism of product chain length determination. J Biol Chem. 2004 Feb 6;279(6):4903-12. Epub 2003 Nov 15. PMID:14617622 doi:10.1074/jbc.M310161200
  3. 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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