View source for 6wum


==Mitochondrial SAM complex - dimer 2 in detergent==
<StructureSection load='6wum' size='340' side='right'caption='[[6wum]], [[Resolution|resolution]] 3.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6wum]] is a 6 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=6WUM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6WUM 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]] 3.6&#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=6wum FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6wum OCA], [https://pdbe.org/6wum PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6wum RCSB], [https://www.ebi.ac.uk/pdbsum/6wum PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6wum 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 6wum" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Thermothelomyces thermophilus]]
[[Category: Botos I]]
[[Category: Diederichs K]]
[[Category: Ni X]]