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| [[Image:1q7b.jpg|left|200px]] | | {{Seed}} |
| | [[Image:1q7b.png|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+'''
| | ===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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_15016358}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 15016358 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_15016358}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Nadp+]] | | [[Category: Nadp+]] |
| [[Category: Oxoacyl reductase]] | | [[Category: Oxoacyl reductase]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:57:32 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 14:17:20 2008'' |
