1q7c
From Proteopedia
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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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==Reference== | ==Reference== | ||
Cofactor-induced conformational rearrangements establish a catalytically competent active site and a proton relay conduit in FabG., Price AC, Zhang YM, Rock CO, White SW, Structure. 2004 Mar;12(3):417-28. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15016358 15016358] | Cofactor-induced conformational rearrangements establish a catalytically competent active site and a proton relay conduit in FabG., Price AC, Zhang YM, Rock CO, White SW, Structure. 2004 Mar;12(3):417-28. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15016358 15016358] | ||
| - | [[Category: 3-oxoacyl-[acyl-carrier-protein] reductase]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: White, S M.]] | [[Category: White, S M.]] | ||
[[Category: Zhang, Y M.]] | [[Category: Zhang, Y M.]] | ||
| - | [[Category: | + | [[Category: Crystal structure]] |
| - | [[Category: | + | [[Category: Nadp+]] |
| - | [[Category: | + | [[Category: Oxoacyl reductase]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:57:29 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 02:57, 3 May 2008
The structure of betaketoacyl-[ACP] reductase Y151F mutant in complex with NADPH fragment
Overview
beta-Ketoacyl-acyl carrier protein reductase (FabG) is a key component in the type II fatty acid synthase system. The structures of Escherichia coli FabG and the FabG[Y151F] mutant in binary complexes with NADP(H) reveal that mechanistically important conformational changes accompany cofactor binding. The active site Ser-Tyr-Lys triad is repositioned into a catalytically competent constellation, and a hydrogen bonded network consisting of ribose hydroxyls, the Ser-Tyr-Lys triad, and four water molecules creates a proton wire to replenish the tyrosine proton donated during catalysis. Also, a disordered loop in FabG forms a substructure in the complex that shapes the entrance to the active site. A key observation is that the nicotinamide portion of the cofactor is disordered in the FabG[Y151F].NADP(H) complex, and Tyr151 appears to be necessary for high-affinity cofactor binding. Biochemical data confirm that FabG[Y151F] is defective in NADPH binding. Finally, structural changes consistent with the observed negative cooperativity of FabG are described.
About this Structure
1Q7C is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Cofactor-induced conformational rearrangements establish a catalytically competent active site and a proton relay conduit in FabG., Price AC, Zhang YM, Rock CO, White SW, Structure. 2004 Mar;12(3):417-28. PMID:15016358 Page seeded by OCA on Sat May 3 05:57:29 2008
