1q7c: Difference between revisions

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New page: left|200px<br /><applet load="1q7c" size="450" color="white" frame="true" align="right" spinBox="true" caption="1q7c, resolution 2.50Å" /> '''The structure of bet...
 
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[[Image:1q7c.jpg|left|200px]]<br /><applet load="1q7c" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1q7c.jpg|left|200px]]<br /><applet load="1q7c" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1q7c, resolution 2.50&Aring;" />
caption="1q7c, resolution 2.50&Aring;" />
'''The structure of betaketoacyl-[ACP] reductase Y151F mutant in complex with NADPH fragment'''<br />
'''The structure of betaketoacyl-[ACP] reductase Y151F mutant in complex with NADPH fragment'''<br />


==Overview==
==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.
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==
==About this Structure==
1Q7C is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with NAP as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/3-oxoacyl-[acyl-carrier-protein]_reductase 3-oxoacyl-[acyl-carrier-protein] reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.100 1.1.1.100] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Q7C OCA].  
1Q7C is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=NAP:'>NAP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/3-oxoacyl-[acyl-carrier-protein]_reductase 3-oxoacyl-[acyl-carrier-protein] reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.100 1.1.1.100] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q7C OCA].  


==Reference==
==Reference==
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Price, A.C.]]
[[Category: Price, A C.]]
[[Category: Rock, C.O.]]
[[Category: Rock, C O.]]
[[Category: White, S.M.]]
[[Category: White, S M.]]
[[Category: Zhang, Y.M.]]
[[Category: Zhang, Y M.]]
[[Category: NAP]]
[[Category: NAP]]
[[Category: oxoacyl reductase; nadp+; crystal structure]]
[[Category: oxoacyl reductase; nadp+; crystal structure]]


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