1fer

<StructureSection load='1fer' size='340' side='right' caption='[[1fer]], [[Resolution|resolution]] 2.30&Aring;' scene=''>

<table><tr><td colspan='2'>[[1fer]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FER OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FER FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=F3S:FE3-S4+CLUSTER'>F3S</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fer FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fer OCA], [http://pdbe.org/1fer PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1fer RCSB], [http://www.ebi.ac.uk/pdbsum/1fer PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1fer ProSAT]</span></td></tr>

[[http://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.

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fe/1fer_consurf.spt"</scriptWhenChecked>

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== Publication Abstract from PubMed ==

Ferredoxin I from Azotobacter vinelandii (AvFdI) is an iron-sulfur protein composed of 106 amino acids, seven Fe atoms and eight inorganic S* atoms. A crystallographic redetermination of its structure showed the originally reported structure to be incorrect. We report here the crystal structure of AvFdI at pH 6.5. Extensive refinement has led to a final R value of 0.170 for all 6986 non-extinct reflections in the range 10-2.3 A using a solvent model which includes 98 discrete solvent atoms with occupancies between 0.3 and 1.0 and an average B value of 22.5 A(2). The first half of the peptide chain closely resembles that of the 55-residue ferredoxin from Peptococcus aerogenes (PaFd), while the remainder consists of three turns of helix and a series of loops which form a cap over part of the molecular core. Despite the similarities in structure and surroundings, the corresponding 4Fe4S* clusters in PaFd and AvFdI have strikingly different redox potentials; a possible explanation has been sought in the differing hydration models for the two molecules.

Structure at pH 6.5 of ferredoxin I from Azotobacter vinelandii at 2.3 A resolution.,Merritt EA, Stout GH, Turley S, Sieker LC, Jehsen LH, Orme-Johnson WH Acta Crystallogr D Biol Crystallogr. 1993 Mar 1;49(Pt 2):272-81. PMID:15299532<ref>PMID:15299532</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1fer" style="background-color:#fffaf0;"></div>

*[[Ferredoxin|Ferredoxin]]

[[Category: Jensen, L H]]

[[Category: Merritt, E A]]

[[Category: Orme-Johnson, W H]]

[[Category: Sieker, L C]]

[[Category: Stout, G H]]

[[Category: Turley, S]]