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[[Image:1f5b.gif|left|200px]]
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{{STRUCTURE_1f5b|  PDB=1f5b  |  SCENE=  }}
'''CRYSTAL STRUCTURE OF F2H FERREDOXIN 1 MUTANT FROM AZOTOBACTER VINELANDII AT 1.75 ANGSTROM RESOLUTION'''


==CRYSTAL STRUCTURE OF F2H FERREDOXIN 1 MUTANT FROM AZOTOBACTER VINELANDII AT 1.75 ANGSTROM RESOLUTION==
<StructureSection load='1f5b' size='340' side='right'caption='[[1f5b]], [[Resolution|resolution]] 1.62&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1f5b]] 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=1F5B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F5B 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]] 1.62&#8491;</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=1f5b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f5b OCA], [https://pdbe.org/1f5b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f5b RCSB], [https://www.ebi.ac.uk/pdbsum/1f5b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f5b ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FER1_AZOVI FER1_AZOVI] Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. This ferredoxin could play a role in regulating gene expression by interacting directly with DNA.
== 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/f5/1f5b_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1f5b ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Elucidating how proteins control the reduction potentials (E0') of [Fe--S] clusters is a longstanding fundamental problem in bioinorganic chemistry. Two site-directed variants of Azotobacter vinelandii ferredoxin I (FdI) that show large shifts in [Fe--S] cluster E0' (100--200 mV versus standard hydrogen electrode (SHE)) have been characterized. High resolution X-ray structures of F2H and F25H variants in their oxidized forms, and circular dichroism (CD) and electron paramagnetic resonance (EPR) of the reduced forms indicate that the overall structure is not affected by the mutations and reveal that there is no increase in solvent accessibility nor any reorientation of backbone amide dipoles or NH--S bonds. The structures, combined with detailed investigation of the variation of E0' with pH and temperature, show that the largest increases in E0' result from the introduction of positive charge due to protonation of the introduced His residues. The smaller (50--100 mV) increases observed for the neutral form are proposed to occur by directing a Hdelta+--Ndelta- dipole toward the reduced form of the cluster.


==Overview==
Crystal structures of ferredoxin variants exhibiting large changes in [Fe-S] reduction potential.,Chen K, Bonagura CA, Tilley GJ, McEvoy JP, Jung YS, Armstrong FA, Stout CD, Burgess BK Nat Struct Biol. 2002 Mar;9(3):188-92. PMID:11875515<ref>PMID:11875515</ref>
Elucidating how proteins control the reduction potentials (E0') of [Fe--S] clusters is a longstanding fundamental problem in bioinorganic chemistry. Two site-directed variants of Azotobacter vinelandii ferredoxin I (FdI) that show large shifts in [Fe--S] cluster E0' (100--200 mV versus standard hydrogen electrode (SHE)) have been characterized. High resolution X-ray structures of F2H and F25H variants in their oxidized forms, and circular dichroism (CD) and electron paramagnetic resonance (EPR) of the reduced forms indicate that the overall structure is not affected by the mutations and reveal that there is no increase in solvent accessibility nor any reorientation of backbone amide dipoles or NH--S bonds. The structures, combined with detailed investigation of the variation of E0' with pH and temperature, show that the largest increases in E0' result from the introduction of positive charge due to protonation of the introduced His residues. The smaller (50--100 mV) increases observed for the neutral form are proposed to occur by directing a Hdelta+--Ndelta- dipole toward the reduced form of the cluster.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1F5B 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=1F5B OCA].
</div>
<div class="pdbe-citations 1f5b" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Crystal structures of ferredoxin variants exhibiting large changes in [Fe-S] reduction potential., Chen K, Bonagura CA, Tilley GJ, McEvoy JP, Jung YS, Armstrong FA, Stout CD, Burgess BK, Nat Struct Biol. 2002 Mar;9(3):188-92. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11875515 11875515]
*[[Ferredoxin 3D structures|Ferredoxin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Azotobacter vinelandii]]
[[Category: Azotobacter vinelandii]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Armstrong, F A.]]
[[Category: Armstrong FA]]
[[Category: Bonagura, C A.]]
[[Category: Bonagura CA]]
[[Category: Burgess, B K.]]
[[Category: Burgess BK]]
[[Category: Chen, K.]]
[[Category: Chen K]]
[[Category: Jung, Y S.]]
[[Category: Jung YS]]
[[Category: Stout, C D.]]
[[Category: Stout CD]]
[[Category: Tilley, G J.]]
[[Category: Tilley GJ]]
[[Category: Beta-sheet]]
[[Category: Ferredoxin]]
[[Category: Iron sulfur protein]]
[[Category: Protein monomer]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 15:55:10 2008''
Retrieved from "https://proteopedia.org/1f5b"