1q7c
From Proteopedia
(New page: 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=" | + | [[Image:1q7c.jpg|left|200px]]<br /><applet load="1q7c" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1q7c, resolution 2.50Å" /> | caption="1q7c, resolution 2.50Å" /> | ||
'''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 | + | 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:// | + | 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 | + | [[Category: Price, A C.]] |
| - | [[Category: Rock, C | + | [[Category: Rock, C O.]] |
| - | [[Category: White, S | + | [[Category: White, S M.]] |
| - | [[Category: Zhang, Y | + | [[Category: Zhang, Y M.]] |
[[Category: NAP]] | [[Category: NAP]] | ||
[[Category: oxoacyl reductase; nadp+; crystal structure]] | [[Category: oxoacyl reductase; nadp+; crystal structure]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:36:39 2008'' |
Revision as of 12:36, 21 February 2008
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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 with as ligand. Active as [acyl-carrier-protein_reductase 3-oxoacyl-[acyl-carrier-protein] reductase], with EC number 1.1.1.100 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 [[Category: 3-oxoacyl-[acyl-carrier-protein] reductase]]
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