This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1q7b
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1q7b.jpg|left|200px]] | + | [[Image:1q7b.jpg|left|200px]] |
| - | + | ||
| - | '''The structure of betaketoacyl-[ACP] reductase from E. coli in complex with NADP+''' | + | {{Structure |
| + | |PDB= 1q7b |SIZE=350|CAPTION= <scene name='initialview01'>1q7b</scene>, resolution 2.05Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <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 from E. coli in complex with NADP+''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1Q7B is a [ | + | 1Q7B 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=1Q7B 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]] | ||
| Line 22: | Line 31: | ||
[[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 13:33:55 2008'' |
Revision as of 11:33, 20 March 2008
| |||||||
| , resolution 2.05Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| 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 from E. coli in complex with NADP+
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
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 [[Category: 3-oxoacyl-[acyl-carrier-protein] reductase]]
Page seeded by OCA on Thu Mar 20 13:33:55 2008
