1q7c: Difference between revisions
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{{STRUCTURE_1q7c| PDB=1q7c | SCENE= }} | {{STRUCTURE_1q7c| PDB=1q7c | SCENE= }} | ||
===The structure of betaketoacyl-[ACP] reductase Y151F mutant in complex with NADPH fragment=== | ===The structure of betaketoacyl-[ACP] reductase Y151F mutant in complex with NADPH fragment=== | ||
{{ABSTRACT_PUBMED_15016358}} | |||
==Function== | |||
[[http://www.uniprot.org/uniprot/FABG_ECOLI FABG_ECOLI]] Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis.<ref>PMID:8631920</ref> <ref>PMID:14996818</ref> | |||
==About this Structure== | ==About this Structure== | ||
[[1q7c]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | [[1q7c]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q7C OCA]. | ||
==Reference== | ==Reference== | ||
<ref group="xtra">PMID:015016358</ref><references group="xtra"/> | <ref group="xtra">PMID:015016358</ref><references group="xtra"/><references/> | ||
[[Category: | [[Category: Bacillus coli migula 1895]] | ||
[[Category: Price, A C.]] | [[Category: Price, A C.]] | ||
[[Category: Rock, C O.]] | [[Category: Rock, C O.]] | ||
Revision as of 12:07, 20 November 2013
The structure of betaketoacyl-[ACP] reductase Y151F mutant in complex with NADPH fragment
Template:ABSTRACT PUBMED 15016358
Function
[FABG_ECOLI] Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis.[1] [2]
About this Structure
1q7c is a 2 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA.
Reference
- Price AC, Zhang YM, Rock CO, White SW. Cofactor-induced conformational rearrangements establish a catalytically competent active site and a proton relay conduit in FabG. Structure. 2004 Mar;12(3):417-28. PMID:15016358 doi:10.1016/j.str.2004.02.008
- ↑ Heath RJ, Rock CO. Inhibition of beta-ketoacyl-acyl carrier protein synthase III (FabH) by acyl-acyl carrier protein in Escherichia coli. J Biol Chem. 1996 May 3;271(18):10996-1000. PMID:8631920
- ↑ Lai CY, Cronan JE. Isolation and characterization of beta-ketoacyl-acyl carrier protein reductase (fabG) mutants of Escherichia coli and Salmonella enterica serovar Typhimurium. J Bacteriol. 2004 Mar;186(6):1869-78. PMID:14996818
