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| | <StructureSection load='2wlb' size='340' side='right'caption='[[2wlb]], [[Resolution|resolution]] 2.60Å' scene=''> | | <StructureSection load='2wlb' size='340' side='right'caption='[[2wlb]], [[Resolution|resolution]] 2.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2wlb]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Cbs_356 Cbs 356]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WLB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2WLB FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2wlb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Schizosaccharomyces_pombe Schizosaccharomyces pombe]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WLB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WLB FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</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]] 2.6Å</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=2wlb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wlb OCA], [http://pdbe.org/2wlb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2wlb RCSB], [http://www.ebi.ac.uk/pdbsum/2wlb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2wlb ProSAT]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</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=2wlb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wlb OCA], [https://pdbe.org/2wlb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wlb RCSB], [https://www.ebi.ac.uk/pdbsum/2wlb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wlb ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/ETP1_SCHPO ETP1_SCHPO] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Cbs 356]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bernhardt, R]] | + | [[Category: Schizosaccharomyces pombe]] |
| - | [[Category: Hannemann, F]] | + | [[Category: Bernhardt R]] |
| - | [[Category: Heinemann, U]] | + | [[Category: Hannemann F]] |
| - | [[Category: Mueller, J J]] | + | [[Category: Heinemann U]] |
| - | [[Category: Schiffler, B]] | + | [[Category: Mueller JJ]] |
| - | [[Category: Adrenodoxin-like]]
| + | [[Category: Schiffler B]] |
| - | [[Category: Electron transport]]
| + | |
| - | [[Category: Ferredoxin]]
| + | |
| - | [[Category: Iron]]
| + | |
| - | [[Category: Iron-sulfur]]
| + | |
| - | [[Category: Metal-binding]]
| + | |
| - | [[Category: Mitochondria]]
| + | |
| - | [[Category: Transport]]
| + | |
| Structural highlights
Function
ETP1_SCHPO
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 protein Etp1 of Schizosaccharomyces pombe consists of an amino-terminal COX15-like domain and a carboxy-terminal ferredoxin-like domain, Etp1(fd), which is cleaved off after mitochondrial import. The physiological function of Etp1(fd) is supposed to lie in the participation in the assembly of iron-sulfur clusters and the synthesis of heme A. In addition, the protein was shown to be the first microbial ferredoxin being able to support electron transfer in mitochondrial steroid hydroxylating cytochrome P450 systems in vivo and in vitro, replacing thereby the native redox partner, adrenodoxin. Despite a sequence similarity of 39% and the fact that fission yeast is a mesophilic organism, thermodynamic studies revealed that Etp1(fd) has a melting temperature more than 20 degrees C higher than adrenodoxin. The three-dimensional structure of Etp1(fd) has been determined by crystallography. To the best of our knowledge it represents the first three-dimensional structure of a yeast ferredoxin. The structure-based sequence alignment of Etp1(fd) with adrenodoxin yields a rational explanation for their observed mutual exchangeability in the cytochrome P450 system. Analysis of the electron exchange with the S. pombe redox partner Arh1 revealed differences between Etp1(fd) and adrenodoxin, which might be linked to their different physiological functions in the mitochondria of mammals and yeast.
Structural and thermodynamic characterization of the adrenodoxin-like domain of the electron-transfer protein Etp1 from Schizosaccharomyces pombe.,Muller JJ, Hannemann F, Schiffler B, Ewen KM, Kappl R, Heinemann U, Bernhardt R J Inorg Biochem. 2011 Apr 9;105(7):957-965. PMID:21536008[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Muller JJ, Hannemann F, Schiffler B, Ewen KM, Kappl R, Heinemann U, Bernhardt R. Structural and thermodynamic characterization of the adrenodoxin-like domain of the electron-transfer protein Etp1 from Schizosaccharomyces pombe. J Inorg Biochem. 2011 Apr 9;105(7):957-965. PMID:21536008 doi:10.1016/j.jinorgbio.2011.04.001
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