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| - | [[Image:1a8p.gif|left|200px]] | |
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| - | {{Structure
| + | ==FERREDOXIN REDUCTASE FROM AZOTOBACTER VINELANDII== |
| - | |PDB= 1a8p |SIZE=350|CAPTION= <scene name='initialview01'>1a8p</scene>, resolution 2.0Å
| + | <StructureSection load='1a8p' size='340' side='right'caption='[[1a8p]], [[Resolution|resolution]] 2.00Å' scene=''> |
| - | |SITE=
| + | == Structural highlights == |
| - | |LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene> | + | <table><tr><td colspan='2'>[[1a8p]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A8P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A8P FirstGlance]. <br> |
| - | |ACTIVITY=
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> |
| - | |GENE=
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr> |
| - | |DOMAIN=
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1a8p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a8p OCA], [https://pdbe.org/1a8p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a8p RCSB], [https://www.ebi.ac.uk/pdbsum/1a8p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a8p ProSAT]</span></td></tr> |
| - | |RELATEDENTRY=
| + | </table> |
| - | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1a8p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a8p OCA], [http://www.ebi.ac.uk/pdbsum/1a8p PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1a8p RCSB]</span>
| + | == Function == |
| - | }}
| + | [https://www.uniprot.org/uniprot/FENR_AZOVI FENR_AZOVI] |
| | + | == Evolutionary Conservation == |
| | + | [[Image:Consurf_key_small.gif|200px|right]] |
| | + | Check<jmol> |
| | + | <jmolCheckbox> |
| | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a8/1a8p_consurf.spt"</scriptWhenChecked> |
| | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | + | <text>to colour the structure by Evolutionary Conservation</text> |
| | + | </jmolCheckbox> |
| | + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1a8p ConSurf]. |
| | + | <div style="clear:both"></div> |
| | | | |
| - | '''FERREDOXIN REDUCTASE FROM AZOTOBACTER VINELANDII'''
| + | ==See Also== |
| - | | + | *[[Ferredoxin 3D structures|Ferredoxin 3D structures]] |
| - | | + | __TOC__ |
| - | ==Overview== | + | </StructureSection> |
| - | 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.
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| - | | + | |
| - | ==About this Structure==
| + | |
| - | 1A8P is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A8P OCA].
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| - | | + | |
| - | ==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:[http://www.ncbi.nlm.nih.gov/pubmed/9865948 9865948]
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| | [[Category: Azotobacter vinelandii]] | | [[Category: Azotobacter vinelandii]] |
| - | [[Category: Single protein]] | + | [[Category: Large Structures]] |
| - | [[Category: Burgess, B K.]] | + | [[Category: Burgess BK]] |
| - | [[Category: Jung, Y S.]] | + | [[Category: Jung YS]] |
| - | [[Category: Kresge, N.]] | + | [[Category: Kresge N]] |
| - | [[Category: Muhlberg, A B.]] | + | [[Category: Muhlberg AB]] |
| - | [[Category: Prasad, G S.]] | + | [[Category: Prasad GS]] |
| - | [[Category: Shaw, A.]] | + | [[Category: Shaw A]] |
| - | [[Category: Stout, C D.]] | + | [[Category: Stout CD]] |
| - | [[Category: oxidoreductase]]
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| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:35:37 2008''
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