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| <StructureSection load='1blu' size='340' side='right'caption='[[1blu]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='1blu' size='340' side='right'caption='[[1blu]], [[Resolution|resolution]] 2.10Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[1blu]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Allochromatium_vinosum Allochromatium vinosum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BLU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BLU FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1blu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Allochromatium_vinosum Allochromatium vinosum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BLU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BLU FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</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=1blu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1blu OCA], [http://pdbe.org/1blu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1blu RCSB], [http://www.ebi.ac.uk/pdbsum/1blu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1blu ProSAT]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[https://proteopedia.org/fgij/fg.htm?mol=1blu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1blu OCA], [https://pdbe.org/1blu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1blu RCSB], [https://www.ebi.ac.uk/pdbsum/1blu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1blu ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function == | | == Function == |
- | [[http://www.uniprot.org/uniprot/FER_ALLVD FER_ALLVD]] Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. | + | [https://www.uniprot.org/uniprot/FER_ALLVD FER_ALLVD] 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]] |
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| [[Category: Allochromatium vinosum]] | | [[Category: Allochromatium vinosum]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Dauter, Z]] | + | [[Category: Dauter Z]] |
- | [[Category: Moulis, J M]] | + | [[Category: Moulis JM]] |
- | [[Category: Sieker, L C]] | + | [[Category: Sieker LC]] |
- | [[Category: Wilson, K S]] | + | [[Category: Wilson KS]] |
- | [[Category: Electron transport]]
| + | |
- | [[Category: Ferredoxin]]
| + | |
| Structural highlights
Function
FER_ALLVD 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 PubMed
The crystal structure of the 2[4Fe-4S] ferredoxin from Chromatium vinosum has been solved by molecular replacement using data recorded with synchrotron radiation. The crystals were hexagonal prisms that showed a strong tendency to develop into long tubes. The hexagonal prisms diffracted to 2.1 A resolution at best, and a structural model for C. vinosum ferredoxin has been built with a final R of 19.2%. The N-terminal domain coordinates the two [4Fe-4S] clusters in a fold that is almost identical to that of other known ferredoxins. However, the structure has two unique features. One is a six-residue insertion between two ligands of one cluster forming a two-turn external loop; this short loop changes the conformation of the Cys 40 ligand compared to other ferredoxins and hampers the building of one NH...S H-bond to one of the inorganic sulfurs. The other remarkable structural element is a 3.5-turn alpha-helix at the C-terminus that covers one side of the same cluster and is linked to the cluster-binding domain by a six-residue external chain segment. The charge distribution is highly asymmetric over the molecule. The structure of C. vinosum ferredoxin strongly suggests divergent evolution for bacterial [3/4Fe-4S] ferredoxins from a common ancestral cluster-binding core. The unexpected slow intramolecular electron transfer rate between the clusters in C. vinosum ferredoxin, compared to other similar proteins, may be attributed to the unusual electronic properties of one of the clusters arising from localized changes in its vicinity rather than to a global structural rearrangement.
Crystal structure of the 2[4Fe-4S] ferredoxin from Chromatium vinosum: evolutionary and mechanistic inferences for [3/4Fe-4S] ferredoxins.,Moulis JM, Sieker LC, Wilson KS, Dauter Z Protein Sci. 1996 Sep;5(9):1765-75. PMID:8880900[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Moulis JM, Sieker LC, Wilson KS, Dauter Z. Crystal structure of the 2[4Fe-4S] ferredoxin from Chromatium vinosum: evolutionary and mechanistic inferences for [3/4Fe-4S] ferredoxins. Protein Sci. 1996 Sep;5(9):1765-75. PMID:8880900
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