6z5u
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Cryo-EM structure of the A. baumannii MlaBDEF complex bound to APPNHP== | |
| + | <StructureSection load='6z5u' size='340' side='right'caption='[[6z5u]], [[Resolution|resolution]] 3.90Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6z5u]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Acinetobacter_baumannii Acinetobacter baumannii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Z5U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6Z5U 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]] 3.9Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</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=6z5u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6z5u OCA], [https://pdbe.org/6z5u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6z5u RCSB], [https://www.ebi.ac.uk/pdbsum/6z5u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6z5u ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/V5V9F4_ACIBA V5V9F4_ACIBA] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Multi-resistant bacteria are a major threat in modern medicine. The gram-negative coccobacillus Acinetobacter baumannii currently leads the WHO list of pathogens in critical need for new therapeutic development. The maintenance of lipid asymmetry (MLA) protein complex is one of the core machineries that transport lipids from/to the outer membrane in gram-negative bacteria. It also contributes to broad-range antibiotic resistance in several pathogens, most prominently in A. baumannii. Nonetheless, the molecular details of its role in lipid transport has remained largely elusive. Here, we report the cryo-EM maps of the core MLA complex, MlaBDEF, from the pathogen A. baumannii, in the apo-, ATP- and ADP-bound states, revealing multiple lipid binding sites in the cytosolic and periplasmic side of the complex. Molecular dynamics simulations suggest their potential trajectory across the membrane. Collectively with the recently-reported structures of the E. coli orthologue, this data also allows us to propose a molecular mechanism of lipid transport by the MLA system. | ||
| - | + | Structure and lipid dynamics in the maintenance of lipid asymmetry inner membrane complex of A. baumannii.,Mann D, Fan J, Somboon K, Farrell DP, Muenks A, Tzokov SB, DiMaio F, Khalid S, Miller SI, Bergeron JRC Commun Biol. 2021 Jun 29;4(1):817. doi: 10.1038/s42003-021-02318-4. PMID:34188171<ref>PMID:34188171</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6z5u" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Acinetobacter baumannii]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Bergeron JRC]] | ||
| + | [[Category: Mann D]] | ||
Current revision
Cryo-EM structure of the A. baumannii MlaBDEF complex bound to APPNHP
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