1go2: Difference between revisions

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[[Category: oxidoreductase]]
[[Category: oxidoreductase]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 11:37:14 2007''
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Revision as of 16:11, 30 October 2007

File:1go2.gif


1go2, resolution 1.7Å

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STRUCTURE OF FERREDOXIN-NADP+ REDUCTASE WITH LYS 72 REPLACED BY GLU (K72E)

OverviewOverview

The three-dimensional structures of K72E, K75R, K75S, K75Q, and K75E, Anabaena Ferredoxin-NADP+ reductase (FNR) mutants have been solved, and, particular structural details of these mutants have been used to assess, the role played by residues 72 and 75 in optimal complex formation and, electron transfer (ET) between FNR and its protein redox partners, Ferredoxin (Fd) and Flavodoxin (Fld). Additionally, because there is no, structural information available on the interaction between FNR and Fld, a, model for the FNR:Fld complex has also been produced based on the, previously reported crystal structures and on that of the rat Cytochrome, P450 reductase (CPR), onto which FNR and Fld have been structurally, aligned, and those reported for the Anabaena and maize FNR:Fd complexes., The model ... [(full description)]

About this StructureAbout this Structure

1GO2 is a [Single protein] structure of sequence from [Anabaena] with SO4 and FAD as [ligands]. Active as [Ferredoxin--NADP(+) reductase], with EC number [1.18.1.2]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

ReferenceReference

Structural analysis of interactions for complex formation between Ferredoxin-NADP+ reductase and its protein partners., Mayoral T, Martinez-Julvez M, Perez-Dorado I, Sanz-Aparicio J, Gomez-Moreno C, Medina M, Hermoso JA, Proteins. 2005 May 15;59(3):592-602. PMID:15789405

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OCA