View source for 6wun


==Mitochondrial SAM complex - dimer 3 in detergent==
<StructureSection load='6wun' size='340' side='right'caption='[[6wun]], [[Resolution|resolution]] 3.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6wun]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermothelomyces_thermophilus Thermothelomyces thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6WUN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6WUN 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]] 3.9&#8491;</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=6wun FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6wun OCA], [https://pdbe.org/6wun PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6wun RCSB], [https://www.ebi.ac.uk/pdbsum/6wun PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6wun ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/G2QAT9_THET4 G2QAT9_THET4] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
In mitochondria, beta-barrel outer membrane proteins mediate protein import, metabolite transport, lipid transport, and biogenesis. The Sorting and Assembly Machinery (SAM) complex consists of three proteins that assemble as a 1:1:1 complex to fold beta-barrel proteins and insert them into the mitochondrial outer membrane. We report cryoEM structures of the SAM complex from Myceliophthora thermophila, which show that Sam50 forms a 16-stranded transmembrane beta-barrel with a single polypeptide-transport-associated (POTRA) domain extending into the intermembrane space. Sam35 and Sam37 are located on the cytosolic side of the outer membrane, with Sam35 capping Sam50, and Sam37 interacting extensively with Sam35. Sam35 and Sam37 each adopt a GST-like fold, with no functional, structural, or sequence similarity to their bacterial counterparts. Structural analysis shows how the Sam50 beta-barrel opens a lateral gate to accommodate its substrates.

Structural insight into mitochondrial beta-barrel outer membrane protein biogenesis.,Diederichs KA, Ni X, Rollauer SE, Botos I, Tan X, King MS, Kunji ERS, Jiang J, Buchanan SK Nat Commun. 2020 Jul 3;11(1):3290. doi: 10.1038/s41467-020-17144-1. PMID:32620929<ref>PMID:32620929</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6wun" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Thermothelomyces thermophilus]]
[[Category: Botos I]]
[[Category: Diederichs K]]
[[Category: Ni X]]