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1q7b

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[[Image:1q7b.jpg|left|200px]]
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{{STRUCTURE_1q7b| PDB=1q7b | SCENE= }}
{{STRUCTURE_1q7b| PDB=1q7b | SCENE= }}
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'''The structure of betaketoacyl-[ACP] reductase from E. coli in complex with NADP+'''
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===The structure of betaketoacyl-[ACP] reductase from E. coli in complex with NADP+===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 15016358 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15016358}}
==About this Structure==
==About this Structure==
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[[Category: Nadp+]]
[[Category: Nadp+]]
[[Category: Oxoacyl reductase]]
[[Category: Oxoacyl reductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:57:32 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 14:17:20 2008''

Revision as of 11:17, 28 July 2008

Image:1q7b.png

Template:STRUCTURE 1q7b

The structure of betaketoacyl-[ACP] reductase from E. coli in complex with NADP+

Template:ABSTRACT PUBMED 15016358

About this Structure

1Q7B 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 Mon Jul 28 14:17:20 2008

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