1fer: Difference between revisions
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<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://www.rcsb.org/pdb/explore.do?structureId=1fer RCSB], [http://www.ebi.ac.uk/pdbsum/1fer PDBsum]</span></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://www.rcsb.org/pdb/explore.do?structureId=1fer RCSB], [http://www.ebi.ac.uk/pdbsum/1fer PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[[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. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 16:27, 25 December 2014
STRUCTURE AT PH 6.5 OF FERREDOXIN I FROM AZOTOBACTER VINELANDII AT 2.3 ANGSTROMS RESOLUTIONSTRUCTURE AT PH 6.5 OF FERREDOXIN I FROM AZOTOBACTER VINELANDII AT 2.3 ANGSTROMS RESOLUTION
Structural highlights
Function[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 Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedFerredoxin 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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