1fca: 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=1fca FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fca OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1fca RCSB], [http://www.ebi.ac.uk/pdbsum/1fca 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=1fca FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fca OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1fca RCSB], [http://www.ebi.ac.uk/pdbsum/1fca PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/FER_CLOAC FER_CLOAC]] Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] |
Revision as of 15:07, 25 December 2014
STRUCTURE OF THE FERREDOXIN FROM CLOSTRIDIUM ACIDURICI: MODEL AT 1.8 ANGSTROMS RESOLUTIONSTRUCTURE OF THE FERREDOXIN FROM CLOSTRIDIUM ACIDURICI: MODEL AT 1.8 ANGSTROMS RESOLUTION
Structural highlights
Function[FER_CLOAC] Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. 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 PubMedFerredoxins (Fd) are electron-carrier proteins, the active sites of which are organized around clusters made of iron and inorganic sulfur. The Fd from Clostridium acidurici is 55 amino acids long and contains two [4Fe-4S] clusters. Crystals have been obtained in the space group P4(3)2(1)2, a = b = 34.441 (5), c = 74.778 (9) A. The structure was solved by molecular replacement using the Fd from Peptostreptcoccus asaccharolyticus as a search model, these two ferredoxins having 37 residues in common. Refinement using molecular-dynamics techniques was then initiated. Successive rounds of model building and refinement gave a structure that includes 45 water molecules with R = 15%. At this stage, the electron-density map clearly revealed discrepancies in the position of two amino acids in the published primary sequence. Refinement based on these modifications led to R = 14.3% for 3921 reflections up to 1.8 A, resolution. The geometry of the two clusters has been found to be in good agreement with that previously obtained at a lower resolution. Interactions of polypeptide chain with the [4Fe-4S] clusters, the cluster geometry as well as the hydrogen bonds involving S, Sgamma, N and water molecules are reported. Structure of the ferredoxin from Clostridium acidurici: model at 1.8 A resolution.,TranQui D, Jesior JC Acta Crystallogr D Biol Crystallogr. 1995 Mar 1;51(Pt 2):155-9. PMID:15299316[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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