3vzz: Difference between revisions
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{{STRUCTURE_3vzz| PDB=3vzz | SCENE= }} | |||
===Crystal structure of PcrB complexed with FsPP from bacillus subtilis subap. subtilis str. 168=== | |||
{{ABSTRACT_PUBMED_23322418}} | |||
==Function== | |||
[[http://www.uniprot.org/uniprot/PCRB_BACSU PCRB_BACSU]] Prenyltransferase that catalyzes in vivo the transfer of the heptaprenyl moiety of heptaprenyl pyrophosphate (HepPP; 35 carbon atoms) to the C3 hydroxyl of sn-glycerol-1-phosphate (G1P), producing heptaprenylglyceryl phosphate (HepGP). This reaction is an ether-bond-formation step in the biosynthesis of archaea-type G1P-based membrane lipids found in Bacillales. To a much lesser extent, is also able to use geranyl diphosphate (GPP; C10) and geranylgeranyl diphosphate (GGPP; C20) as the prenyl donors, but not farnesyl pyrophosphate (FPP; C15). Can not use glycerol-3-phosphate (G3P) or 3-phosphoglycerate (3PG) as an acceptor.<ref>PMID:18558723</ref> <ref>PMID:21761520</ref> <ref>PMID:21214173</ref> | |||
==About this Structure== | |||
[[3vzz]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VZZ OCA]. | |||
==Reference== | |||
<ref group="xtra">PMID:023322418</ref><references group="xtra"/><references/> | |||
[[Category: Bacillus subtilis subsp. subtilis str. 168]] | |||
[[Category: Chan, H C.]] | |||
[[Category: Chen, C C.]] | |||
[[Category: Feng, X.]] | |||
[[Category: Guo, R T.]] | |||
[[Category: He, M.]] | |||
[[Category: Hu, Y.]] | |||
[[Category: Huang, C H.]] | |||
[[Category: Ko, T P.]] | |||
[[Category: Li, Y.]] | |||
[[Category: Liu, Y L.]] | |||
[[Category: Oldfield, E.]] | |||
[[Category: Pang, X.]] | |||
[[Category: Ren, F.]] | |||
[[Category: Wang, K.]] | |||
[[Category: Biosynthesis]] | |||
[[Category: Enzyme catalysis]] | |||
[[Category: Prenyltransferase]] | |||
[[Category: Transferase]] | |||
Revision as of 06:38, 1 August 2013
Crystal structure of PcrB complexed with FsPP from bacillus subtilis subap. subtilis str. 168Crystal structure of PcrB complexed with FsPP from bacillus subtilis subap. subtilis str. 168
Template:ABSTRACT PUBMED 23322418
FunctionFunction
[PCRB_BACSU] Prenyltransferase that catalyzes in vivo the transfer of the heptaprenyl moiety of heptaprenyl pyrophosphate (HepPP; 35 carbon atoms) to the C3 hydroxyl of sn-glycerol-1-phosphate (G1P), producing heptaprenylglyceryl phosphate (HepGP). This reaction is an ether-bond-formation step in the biosynthesis of archaea-type G1P-based membrane lipids found in Bacillales. To a much lesser extent, is also able to use geranyl diphosphate (GPP; C10) and geranylgeranyl diphosphate (GGPP; C20) as the prenyl donors, but not farnesyl pyrophosphate (FPP; C15). Can not use glycerol-3-phosphate (G3P) or 3-phosphoglycerate (3PG) as an acceptor.[1] [2] [3]
About this StructureAbout this Structure
3vzz is a 2 chain structure with sequence from Bacillus subtilis subsp. subtilis str. 168. Full crystallographic information is available from OCA.
ReferenceReference
- ↑ Ren F, Feng X, Ko TP, Huang CH, Hu Y, Chan HC, Liu YL, Wang K, Chen CC, Pang X, He M, Li Y, Oldfield E, Guo RT. Insights into TIM-barrel prenyl transferase mechanisms: crystal structures of PcrB from Bacillus subtilis and Staphylococcus aureus. Chembiochem. 2013 Jan 21;14(2):195-9. doi: 10.1002/cbic.201200748. Epub 2013 Jan , 15. PMID:23322418 doi:10.1002/cbic.201200748
- ↑ Guldan H, Sterner R, Babinger P. Identification and characterization of a bacterial glycerol-1-phosphate dehydrogenase: Ni(2+)-dependent AraM from Bacillus subtilis. Biochemistry. 2008 Jul 15;47(28):7376-84. Epub 2008 Jun 18. PMID:18558723 doi:10.1021/bi8005779
- ↑ Guldan H, Matysik FM, Bocola M, Sterner R, Babinger P. Functional assignment of an enzyme that catalyzes the synthesis of an archaea-type ether lipid in bacteria. Angew Chem Int Ed Engl. 2011 Aug 22;50(35):8188-91. doi: 10.1002/anie.201101832. , Epub 2011 Jul 14. PMID:21761520 doi:10.1002/anie.201101832
- ↑ Doud EH, Perlstein DL, Wolpert M, Cane DE, Walker S. Two distinct mechanisms for TIM barrel prenyltransferases in bacteria. J Am Chem Soc. 2011 Feb 9;133(5):1270-3. doi: 10.1021/ja109578b. Epub 2011 Jan 7. PMID:21214173 doi:10.1021/ja109578b