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| | {{STRUCTURE_1a8p| PDB=1a8p | SCENE= }} | | {{STRUCTURE_1a8p| PDB=1a8p | SCENE= }} |
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| - | '''FERREDOXIN REDUCTASE FROM AZOTOBACTER VINELANDII'''
| + | ===FERREDOXIN REDUCTASE FROM AZOTOBACTER VINELANDII=== |
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| - | ==Overview==
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| - | NADPH:ferredoxin reductase (AvFPR) is involved in the response to oxidative stress in Azotobacter vinelandii. The crystal structure of AvFPR has been determined at 2.0 A resolution. The polypeptide fold is homologous with six other oxidoreductases whose structures have been solved including Escherichia coli flavodoxin reductase (EcFldR) and spinach, and Anabaena ferredoxin:NADP+ reductases (FNR). AvFPR is overall most homologous to EcFldR. The structure is comprised of a N-terminal six-stranded antiparallel beta-barrel domain, which binds FAD, and a C-terminal five-stranded parallel beta-sheet domain, which binds NADPH/NADP+ and has a classical nucleotide binding fold. The two domains associate to form a deep cleft where the NADPH and FAD binding sites are juxtaposed. The structure displays sequence conserved motifs in the region surrounding the two dinucleotide binding sites, which are characteristic of the homologous enzymes. The folded over conformation of FAD in AvFPR is similar to that in EcFldR due to stacking of Phe255 on the adenine ring of FAD, but it differs from that in the FNR enzymes, which lack a homologous aromatic residue. The structure of AvFPR displays three unique features in the environment of the bound FAD. Two features may affect the rate of reduction of FAD: the absence of an aromatic residue stacked on the isoalloxazine ring in the NADPH binding site; and the interaction of a carbonyl group with N10 of the flavin. Both of these features are due to the substitution of a conserved C-terminal tyrosine residue with alanine (Ala254) in AvFPR. An additional unique feature may affect the interaction of AvFPR with its redox partner ferredoxin I (FdI). This is the extension of the C-terminus by three residues relative to EcFldR and by four residues relative to FNR. The C-terminal residue, Lys258, interacts with the AMP phosphate of FAD. Consequently, both phosphate groups are paired with a basic group due to the simultaneous interaction of the FMN phosphate with Arg51 in a conserved FAD binding motif. The fourth feature, common to homologous oxidoreductases, is a concentration of 10 basic residues on the face of the protein surrounding the active site, in addition to Arg51 and Lys258.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_9865948}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 9865948 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_9865948}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Stout, C D.]] | | [[Category: Stout, C D.]] |
| | [[Category: Oxidoreductase]] | | [[Category: Oxidoreductase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 09:59:03 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 16:23:28 2008'' |
Revision as of 13:23, 30 June 2008
Template:STRUCTURE 1a8p
FERREDOXIN REDUCTASE FROM AZOTOBACTER VINELANDII
Template:ABSTRACT PUBMED 9865948
About this Structure
1A8P is a Single protein structure of sequence from Azotobacter vinelandii. Full crystallographic information is available from OCA.
Reference
The crystal structure of NADPH:ferredoxin reductase from Azotobacter vinelandii., Sridhar Prasad G, Kresge N, Muhlberg AB, Shaw A, Jung YS, Burgess BK, Stout CD, Protein Sci. 1998 Dec;7(12):2541-9. PMID:9865948
Page seeded by OCA on Mon Jun 30 16:23:28 2008
