View source for 8dck


==Structure of hemolysin A secretion system HlyB/D complex, ATP-bound==
<StructureSection load='8dck' size='340' side='right'caption='[[8dck]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8dck]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_CFT073 Escherichia coli CFT073]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8DCK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8DCK 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]] 3.4&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</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=8dck FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8dck OCA], [https://pdbe.org/8dck PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8dck RCSB], [https://www.ebi.ac.uk/pdbsum/8dck PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8dck ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/HLYB_ECOL6 HLYB_ECOL6] Part of the ABC transporter complex HlyBD involved in hemolysin export. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation (By similarity).
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Type 1 secretion systems (T1SSs) are widespread in pathogenic Gram-negative bacteria, extruding protein substrates following synthesis of the entire polypeptide. The Escherichia coli hemolysin A secretion system has long been considered a prototype in structural and mechanistic studies of T1SSs. Three membrane proteins-an inner membrane ABC transporter HlyB, an adaptor protein HlyD, and an outer membrane porin TolC-are required for secretion. However, the stoichiometry and structure of the complex are unknown. Here, cryo-electron microscopy (cryo-EM) structures determined in two conformations reveal that the inner membrane complex is a hetero-dodecameric assembly comprising three HlyB homodimers and six HlyD subunits. Functional studies indicate that oligomerization of HlyB and HlyD is essential for protein secretion and that polypeptides translocate through a canonical ABC transporter pathway in HlyB. Our data suggest that T1SSs entail three ABC transporters, one that functions as a protein channel and two that allosterically power the translocation process.

The hemolysin A secretion system is a multi-engine pump containing three ABC transporters.,Zhao H, Lee J, Chen J Cell. 2022 Sep 1;185(18):3329-3340.e13. doi: 10.1016/j.cell.2022.07.017. PMID:36055198<ref>PMID:36055198</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8dck" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli CFT073]]
[[Category: Large Structures]]
[[Category: Chen J]]
[[Category: Zhao H]]