View source for 7nnt


==Cryo-EM structure of the folate-specific ECF transporter complex in DDM micelles==
<StructureSection load='7nnt' size='340' side='right'caption='[[7nnt]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7nnt]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Lactobacillus_delbrueckii_subsp._bulgaricus_ATCC_11842_=_JCM_1002 Lactobacillus delbrueckii subsp. bulgaricus ATCC 11842 = JCM 1002]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7NNT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7NNT 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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7nnt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7nnt OCA], [https://pdbe.org/7nnt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7nnt RCSB], [https://www.ebi.ac.uk/pdbsum/7nnt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7nnt ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ECFA1_LACDA ECFA1_LACDA] ATP-binding (A) component of a common energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates.
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== Publication Abstract from PubMed ==
Energy-coupling factor (ECF)-type transporters are small, asymmetric membrane protein complexes ( approximately 115 kDa) that consist of a membrane-embedded, substrate-binding protein (S component) and a tripartite ATP-hydrolyzing module (ECF module). They import micronutrients into bacterial cells and have been proposed to use a highly unusual transport mechanism, in which the substrate is dragged across the membrane by a toppling motion of the S component. However, it remains unclear how the lipid bilayer could accommodate such a movement. Here, we used cryogenic electron microscopy at 200 kV to determine structures of a folate-specific ECF transporter in lipid nanodiscs and detergent micelles at 2.7- and 3.4-A resolution, respectively. The structures reveal an irregularly shaped bilayer environment around the membrane-embedded complex and suggest that toppling of the S component is facilitated by protein-induced membrane deformations. In this way, structural remodeling of the lipid bilayer environment is exploited to guide the transport process.

Insights into the bilayer-mediated toppling mechanism of a folate-specific ECF transporter by cryo-EM.,Thangaratnarajah C, Rheinberger J, Paulino C, Slotboom DJ Proc Natl Acad Sci U S A. 2021 Aug 24;118(34):e2105014118. doi: , 10.1073/pnas.2105014118. PMID:34408021<ref>PMID:34408021</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
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</StructureSection>
[[Category: Lactobacillus delbrueckii subsp. bulgaricus ATCC 11842 = JCM 1002]]
[[Category: Large Structures]]
[[Category: Paulino C]]
[[Category: Rheinberger J]]
[[Category: Slotboom DJ]]
[[Category: Thangaratnarajah C]]