|
|
| Line 3: |
Line 3: |
| | <SX load='6sh5' size='340' side='right' viewer='molstar' caption='[[6sh5]], [[Resolution|resolution]] 4.60Å' scene=''> | | <SX load='6sh5' size='340' side='right' viewer='molstar' caption='[[6sh5]], [[Resolution|resolution]] 4.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6sh5]] is a 7 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SH5 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6SH5 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6sh5]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SH5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6SH5 FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6sh5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sh5 OCA], [http://pdbe.org/6sh5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6sh5 RCSB], [http://www.ebi.ac.uk/pdbsum/6sh5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6sh5 ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.6Å</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=6sh5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sh5 OCA], [https://pdbe.org/6sh5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6sh5 RCSB], [https://www.ebi.ac.uk/pdbsum/6sh5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6sh5 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/BCS1_YEAST BCS1_YEAST]] Essential for the expression of the Rieske iron-sulfur protein. | + | [https://www.uniprot.org/uniprot/BCS1_YEAST BCS1_YEAST] Essential for the expression of the Rieske iron-sulfur protein. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 23: |
Line 24: |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Saccharomyces cerevisiae]] | | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Beckmann, R]] | + | [[Category: Beckmann R]] |
| - | [[Category: Kater, L]] | + | [[Category: Kater L]] |
| - | [[Category: Inner mitochondiral membrane]]
| + | |
| - | [[Category: Mitochondira]]
| + | |
| - | [[Category: Rieske]]
| + | |
| - | [[Category: Translocase]]
| + | |
| - | [[Category: Translocation]]
| + | |
| Structural highlights
Function
BCS1_YEAST Essential for the expression of the Rieske iron-sulfur protein.
Publication Abstract from PubMed
Some proteins require completion of folding before translocation across a membrane into another cellular compartment. Yet the permeability barrier of the membrane should not be compromised and mechanisms have remained mostly elusive. Here, we present the structure of Saccharomyces cerevisiae Bcs1, an AAA-ATPase of the inner mitochondrial membrane. Bcs1 facilitates the translocation of the Rieske protein, Rip1, which requires folding and incorporation of a 2Fe-2S cluster before translocation and subsequent integration into the bc1 complex. Surprisingly, Bcs1 assembles into exclusively heptameric homo-oligomers, with each protomer consisting of an amphipathic transmembrane helix, a middle domain and an ATPase domain. Together they form two aqueous vestibules, the first being accessible from the mitochondrial matrix and the second positioned in the inner membrane, with both separated by the seal-forming middle domain. On the basis of this unique architecture, we propose an airlock-like translocation mechanism for folded Rip1.
Structure of the Bcs1 AAA-ATPase suggests an airlock-like translocation mechanism for folded proteins.,Kater L, Wagener N, Berninghausen O, Becker T, Neupert W, Beckmann R Nat Struct Mol Biol. 2020 Feb;27(2):142-149. doi: 10.1038/s41594-019-0364-1. Epub, 2020 Jan 27. PMID:31988523[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kater L, Wagener N, Berninghausen O, Becker T, Neupert W, Beckmann R. Structure of the Bcs1 AAA-ATPase suggests an airlock-like translocation mechanism for folded proteins. Nat Struct Mol Biol. 2020 Feb;27(2):142-149. doi: 10.1038/s41594-019-0364-1. Epub, 2020 Jan 27. PMID:31988523 doi:http://dx.doi.org/10.1038/s41594-019-0364-1
|
