View source for 6xgz


==Crystal structure of E. coli MlaFB ABC transport subunits in the monomeric state==
<StructureSection load='6xgz' size='340' side='right'caption='[[6xgz]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6xgz]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [https://en.wikipedia.org/wiki/Escherichia_coli_LAU-EC10 Escherichia coli LAU-EC10]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6XGZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6XGZ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=6xgz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xgz OCA], [https://pdbe.org/6xgz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6xgz RCSB], [https://www.ebi.ac.uk/pdbsum/6xgz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6xgz ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MLAF_ECOLI MLAF_ECOLI] Part of the ABC transporter complex MlaFEDB, which is involved in a phospholipid transport pathway that maintains lipid asymmetry in the outer membrane by retrograde trafficking of phospholipids from the outer membrane to the inner membrane. Responsible for energy coupling to the transport system.<ref>PMID:19383799</ref> <ref>PMID:27529189</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
ABC transporters facilitate the movement of diverse molecules across cellular membranes, but how their activity is regulated post-translationally is not well understood. Here we report the crystal structure of MlaFB from E. coli, the cytoplasmic portion of the larger MlaFEDB ABC transporter complex, which drives phospholipid trafficking across the bacterial envelope to maintain outer membrane integrity. MlaB, a STAS domain protein, binds the ABC nucleotide binding domain, MlaF, and is required for its stability. Our structure also implicates a unique C-terminal tail of MlaF in self-dimerization. Both the C-terminal tail of MlaF and the interaction with MlaB are required for the proper assembly of the MlaFEDB complex and its function in cells. This work leads to a new model for how an important bacterial lipid transporter may be regulated by small proteins, and raises the possibility that similar regulatory mechanisms may exist more broadly across the ABC transporter family.

Structure of MlaFB uncovers novel mechanisms of ABC transporter regulation.,Kolich LR, Chang YT, Coudray N, Giacometti SI, MacRae MR, Isom GL, Teran EM, Bhabha G, Ekiert DC Elife. 2020 Jun 30;9:e60030. doi: 10.7554/eLife.60030. PMID:32602838<ref>PMID:32602838</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6xgz" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli LAU-EC10]]
[[Category: Large Structures]]
[[Category: Bhabha G]]
[[Category: Chang Y]]
[[Category: Ekiert DC]]