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| | <SX load='6uks' size='340' side='right' viewer='molstar' caption='[[6uks]], [[Resolution|resolution]] 3.20Å' scene=''> | | <SX load='6uks' size='340' side='right' viewer='molstar' caption='[[6uks]], [[Resolution|resolution]] 3.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6uks]] is a 7 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6UKS OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6UKS FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6uks]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6UKS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6UKS FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AGS:PHOSPHOTHIOPHOSPHORIC+ACID-ADENYLATE+ESTER'>AGS</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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]] 3.2Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Bcs1l ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AGS:PHOSPHOTHIOPHOSPHORIC+ACID-ADENYLATE+ESTER'>AGS</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=6uks FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6uks OCA], [http://pdbe.org/6uks PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6uks RCSB], [http://www.ebi.ac.uk/pdbsum/6uks PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6uks ProSAT]</span></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=6uks FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6uks OCA], [https://pdbe.org/6uks PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6uks RCSB], [https://www.ebi.ac.uk/pdbsum/6uks PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6uks ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/BCS1_MOUSE BCS1_MOUSE]] Chaperone necessary for the assembly of mitochondrial respiratory chain complex III. Plays an important role in the maintenance of mitochondrial tubular networks, respiratory chain assembly and formation of the LETM1 complex (By similarity). | + | [https://www.uniprot.org/uniprot/BCS1_MOUSE BCS1_MOUSE] Chaperone necessary for the assembly of mitochondrial respiratory chain complex III. Plays an important role in the maintenance of mitochondrial tubular networks, respiratory chain assembly and formation of the LETM1 complex (By similarity). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </SX> | | </SX> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Mus musculus]] |
| - | [[Category: Borgnia, M J]] | + | [[Category: Borgnia MJ]] |
| - | [[Category: Hsu, A L]] | + | [[Category: Hsu AL]] |
| - | [[Category: Tang, W K]] | + | [[Category: Tang WK]] |
| - | [[Category: Xia, D]] | + | [[Category: Xia D]] |
| - | [[Category: Aaa atpase]]
| + | |
| - | [[Category: Bcs1]]
| + | |
| - | [[Category: Chaperone]]
| + | |
| - | [[Category: Mitochondrial inner membrane]]
| + | |
| Structural highlights
Function
BCS1_MOUSE Chaperone necessary for the assembly of mitochondrial respiratory chain complex III. Plays an important role in the maintenance of mitochondrial tubular networks, respiratory chain assembly and formation of the LETM1 complex (By similarity).
Publication Abstract from PubMed
The mitochondrial membrane-bound AAA protein Bcs1 translocate substrates across the mitochondrial inner membrane without previous unfolding. One substrate of Bcs1 is the iron-sulfur protein (ISP), a subunit of the respiratory Complex III. How Bcs1 translocates ISP across the membrane is unknown. Here we report structures of mouse Bcs1 in two different conformations, representing three nucleotide states. The apo and ADP-bound structures reveal a homo-heptamer and show a large putative substrate-binding cavity accessible to the matrix space. ATP binding drives a contraction of the cavity by concerted motion of the ATPase domains, which could push substrate across the membrane. Our findings shed light on the potential mechanism of translocating folded proteins across a membrane, offer insights into the assembly process of Complex III and allow mapping of human disease-associated mutations onto the Bcs1 structure.
Structures of AAA protein translocase Bcs1 suggest translocation mechanism of a folded protein.,Tang WK, Borgnia MJ, Hsu AL, Esser L, Fox T, de Val N, Xia D Nat Struct Mol Biol. 2020 Feb;27(2):202-209. doi: 10.1038/s41594-020-0373-0. Epub, 2020 Feb 10. PMID:32042153[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Tang WK, Borgnia MJ, Hsu AL, Esser L, Fox T, de Val N, Xia D. Structures of AAA protein translocase Bcs1 suggest translocation mechanism of a folded protein. Nat Struct Mol Biol. 2020 Feb;27(2):202-209. doi: 10.1038/s41594-020-0373-0. Epub, 2020 Feb 10. PMID:32042153 doi:http://dx.doi.org/10.1038/s41594-020-0373-0
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