View source for 8bmr


==Cryo-EM structure of the wild-type solitary ECF module in MSP2N2 lipid nanodiscs in the ATPase open and nucleotide-free conformation==
<StructureSection load='8bmr' size='340' side='right'caption='[[8bmr]], [[Resolution|resolution]] 3.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8bmr]] is a 3 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=8BMR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8BMR 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]] 3.8&#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=8bmr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8bmr OCA], [https://pdbe.org/8bmr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8bmr RCSB], [https://www.ebi.ac.uk/pdbsum/8bmr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8bmr 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.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Energy-coupling factor (ECF)-type transporters mediate the uptake of micronutrients in many bacteria. They consist of a substrate-translocating subunit (S-component) and an ATP-hydrolysing motor (ECF module) Previous data indicate that the S-component topples within the membrane to alternately expose the binding site to either side of the membrane. In many ECF transporters, the substrate-free S-component can be expelled from the ECF module. Here we study this enigmatic expulsion step by cryogenic electron microscopy and reveal that ATP induces a concave-to-convex shape change of two long helices in the motor, thereby destroying the S-component's docking site and allowing for its dissociation. We show that adaptation of the membrane morphology to the conformational state of the motor may favour expulsion of the substrate-free S-component when ATP is bound and docking of the substrate-loaded S-component after hydrolysis. Our work provides a picture of bilayer-assisted chemo-mechanical coupling in the transport cycle of ECF transporters.

Expulsion mechanism of the substrate-translocating subunit in ECF transporters.,Thangaratnarajah C, Nijland M, Borges-Araujo L, Jeucken A, Rheinberger J, Marrink SJ, Souza PCT, Paulino C, Slotboom DJ Nat Commun. 2023 Jul 25;14(1):4484. doi: 10.1038/s41467-023-40266-1. PMID:37491368<ref>PMID:37491368</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8bmr" style="background-color:#fffaf0;"></div>
== 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]]