1yob
From Proteopedia
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(New page: 200px<br /><applet load="1yob" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yob, resolution 2.25Å" /> '''C69A Flavodoxin II f...) |
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| - | [[Image:1yob.gif|left|200px]]<br /><applet load="1yob" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1yob, resolution 2.25Å" /> | ||
| - | '''C69A Flavodoxin II from Azotobacter vinelandii'''<br /> | ||
| - | == | + | ==C69A Flavodoxin II from Azotobacter vinelandii== |
| - | Flavodoxin II from Azotobacter vinelandii is a "long-chain" flavodoxin and | + | <StructureSection load='1yob' size='340' side='right'caption='[[1yob]], [[Resolution|resolution]] 2.25Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1yob]] is a 2 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=1YOB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YOB FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.25Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1yob FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yob OCA], [https://pdbe.org/1yob PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yob RCSB], [https://www.ebi.ac.uk/pdbsum/1yob PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yob ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/FLAV_AZOVI FLAV_AZOVI] Low-potential electron donor to a number of redox enzymes. NifF is the electron donor to nitrogenase. | ||
| + | == 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/yo/1yob_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=1yob ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Flavodoxin II from Azotobacter vinelandii is a "long-chain" flavodoxin and has one of the lowest E1 midpoint potentials found within the flavodoxin family. To better understand the relationship between structural features and redox potentials, the oxidized form of the C69A mutant of this flavodoxin was crystallized and its three-dimensional structure determined to a resolution of 2.25 A by molecular replacement. Its overall fold is similar to that of other flavodoxins, with a central five-stranded parallel beta-sheet flanked on either side by alpha-helices. An eight-residue insertion, compared with other long-chain flavodoxins, forms a short 3(10) helix preceding the start of the alpha3 helix. The flavin mononucleotide (FMN) cofactor is flanked by a leucine on its re face instead of the more conserved tryptophan, resulting in a more solvent-accessible FMN binding site and stabilization of the hydroquinone (hq) state. In particular the absence of a hydrogen bond to the N5 atom of the oxidized FMN was identified, which destabilizes the ox form, as well as an exceptionally large patch of acidic residues in the vicinity of the FMN N1 atom, which destabilizes the hq form. It is also argued that the presence of a Gly at position 58 in the sequence stabilizes the semiquinone (sq) form, as a result, raising the E2 value in particular. | ||
| - | + | A crystallographic study of Cys69Ala flavodoxin II from Azotobacter vinelandii: structural determinants of redox potential.,Alagaratnam S, van Pouderoyen G, Pijning T, Dijkstra BW, Cavazzini D, Rossi GL, Van Dongen WM, van Mierlo CP, van Berkel WJ, Canters GW Protein Sci. 2005 Sep;14(9):2284-95. PMID:16131657<ref>PMID:16131657</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1yob" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[Flavodoxin 3D structures|Flavodoxin 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Azotobacter vinelandii]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Alagaratnam S]] | ||
| + | [[Category: Canters GW]] | ||
| + | [[Category: Cavazzini D]] | ||
| + | [[Category: Dijkstra BW]] | ||
| + | [[Category: Pijning T]] | ||
| + | [[Category: Rossi GL]] | ||
| + | [[Category: Van Pouderoyen G]] | ||
Current revision
C69A Flavodoxin II from Azotobacter vinelandii
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