Undecaprenyl pyrophosphate synthase

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<StructureSection load='1x07' size='450' side='right' caption='Structure of E. coli UPP complex with isopentenyl pyrophosphate, phosphate and Mg+2 (green) (PDB code [[1x07]]).' scene='' pspeed='8'>
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<StructureSection load='1x07' size='450' side='right' caption='Structure of E. coli UPP complex with isopentenyl pyrophosphate, phosphate and Mg+2 (green) (PDB code [[1x07]]).' scene='59/591995/Cv/4' pspeed='8'>
== Function ==
== Function ==

Revision as of 12:54, 26 March 2017

Structure of E. coli UPP complex with isopentenyl pyrophosphate, phosphate and Mg+2 (green) (PDB code 1x07).

Drag the structure with the mouse to rotate

3D structures of undecaprenyl pyrophosphate synthase

Updated on 26-March-2017

References

  1. Guo RT, Ko TP, Chen AP, Kuo CJ, Wang AH, Liang PH. Crystal structures of undecaprenyl pyrophosphate synthase in complex with magnesium, isopentenyl pyrophosphate, and farnesyl thiopyrophosphate: roles of the metal ion and conserved residues in catalysis. J Biol Chem. 2005 May 27;280(21):20762-74. Epub 2005 Mar 23. PMID:15788389 doi:10.1074/jbc.M502121200
  2. Jukic M, Rozman K, Gobec S. Recent Advances in the Development of Undecaprenyl Pyrophosphate Synthase Inhibitors as Potential Antibacterials. Curr Med Chem. 2016;23(5):464-82. PMID:26718796
  3. Guo RT, Ko TP, Chen AP, Kuo CJ, Wang AH, Liang PH. Crystal structures of undecaprenyl pyrophosphate synthase in complex with magnesium, isopentenyl pyrophosphate, and farnesyl thiopyrophosphate: roles of the metal ion and conserved residues in catalysis. J Biol Chem. 2005 May 27;280(21):20762-74. Epub 2005 Mar 23. PMID:15788389 doi:10.1074/jbc.M502121200

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Michal Harel, Alexander Berchansky

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