View source for 6uks


==ATPgammaS bound mBcs1==
<SX load='6uks' size='340' side='right' viewer='molstar' caption='[[6uks]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
== Structural highlights ==
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.2&#8491;</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'>[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>
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== Function ==
[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).
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== 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<ref>PMID:32042153</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 6uks" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Borgnia MJ]]
[[Category: Hsu AL]]
[[Category: Tang WK]]
[[Category: Xia D]]