7znu

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Current revision (06:42, 24 July 2024) (edit) (undo)
 
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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[7znu]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Brucella_abortus_2308 Brucella abortus 2308]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7ZNU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ZNU FirstGlance]. <br>
<table><tr><td colspan='2'>[[7znu]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Brucella_abortus_2308 Brucella abortus 2308]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7ZNU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ZNU FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=VO4:VANADATE+ION'>VO4</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=VO4:VANADATE+ION'>VO4</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=7znu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7znu OCA], [https://pdbe.org/7znu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7znu RCSB], [https://www.ebi.ac.uk/pdbsum/7znu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7znu ProSAT]</span></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=7znu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7znu OCA], [https://pdbe.org/7znu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7znu RCSB], [https://www.ebi.ac.uk/pdbsum/7znu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7znu ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[https://www.uniprot.org/uniprot/NDVA_BRUA2 NDVA_BRUA2] Involved in beta-(1-->2)glucan export. Its export to the periplasmic space is required to exert its action as a virulence factor. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation (Probable).<ref>PMID:15039351</ref>
[https://www.uniprot.org/uniprot/NDVA_BRUA2 NDVA_BRUA2] Involved in beta-(1-->2)glucan export. Its export to the periplasmic space is required to exert its action as a virulence factor. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation (Probable).<ref>PMID:15039351</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Polysaccharides play critical roles in bacteria, including the formation of protective capsules and biofilms and establishing specific host cell interactions. Their transport across membranes is often mediated by ATP-binding cassette (ABC) transporters, which utilize ATP to translocate diverse molecules. Cyclic beta-glucans (CbetaGs) are critical for host interaction of the Rhizobiales, including the zoonotic pathogen Brucella. CbetaGs are exported into the periplasmic space by the cyclic glucan transporter (Cgt). The interaction of an ABC transporter with a polysaccharide substrate has not been visualized so far. Here we use single-particle cryoelectron microscopy to elucidate the structures of Cgt from Brucella abortus in four conformational states. The substrate-bound structure reveals an unusual binding pocket at the height of the cytoplasmic leaflet, whereas ADP-vanadate models hint at an alternative mechanism of substrate release. Our work provides insights into the translocation of large, heterogeneous substrates and sheds light on protein-polysaccharide interactions in general.
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Mechanism of cyclic beta-glucan export by ABC transporter Cgt of Brucella.,Sedzicki J, Ni D, Lehmann F, Wu N, Zenobi R, Jung S, Stahlberg H, Dehio C Nat Struct Mol Biol. 2022 Dec;29(12):1170-1177. doi: 10.1038/s41594-022-00868-7. , Epub 2022 Dec 1. PMID:36456825<ref>PMID:36456825</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 7znu" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>

Current revision

cryo-EM structure of CGT ABC transporter in detergent micelle

PDB ID 7znu

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