1q7c

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[[Image:1q7c.png|left|200px]]
 
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{{STRUCTURE_1q7c| PDB=1q7c | SCENE= }}
{{STRUCTURE_1q7c| PDB=1q7c | SCENE= }}
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===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===
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{{ABSTRACT_PUBMED_15016358}}
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{{ABSTRACT_PUBMED_15016358}}
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==Function==
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[[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==
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[[1q7c]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q7C OCA].
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[[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==
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<ref group="xtra">PMID:015016358</ref><references group="xtra"/>
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<ref group="xtra">PMID:015016358</ref><references group="xtra"/><references/>
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[[Category: Escherichia coli]]
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[[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

Template:STRUCTURE 1q7c

Contents

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
  1. ↑ 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
  2. ↑ 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

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