1q7c: Difference between revisions
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'''The structure of betaketoacyl-[ACP] reductase Y151F mutant in complex with NADPH fragment''' | {{Structure | ||
|PDB= 1q7c |SIZE=350|CAPTION= <scene name='initialview01'>1q7c</scene>, resolution 2.50Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=NAP:NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE'>NAP</scene> | |||
|ACTIVITY= [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] | |||
|GENE= | |||
}} | |||
'''The structure of betaketoacyl-[ACP] reductase Y151F mutant in complex with NADPH fragment''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1Q7C is a [ | 1Q7C is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q7C OCA]. | ||
==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:// | 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: 3-oxoacyl-[acyl-carrier-protein] reductase]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
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[[Category: oxoacyl reductase; nadp+; crystal structure]] | [[Category: oxoacyl reductase; nadp+; crystal structure]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:33:53 2008'' | ||
Revision as of 11:33, 20 March 2008
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| 1q7c, resolution 2.50Å | |||||||||||||
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| Ligands: | NAP | ||||||||||||
| Activity: | [acyl-carrier-protein_reductase 3-oxoacyl-[acyl-carrier-protein] reductase], with EC number 1.1.1.100 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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 [[Category: 3-oxoacyl-[acyl-carrier-protein] reductase]]
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