6p6i: Difference between revisions
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==Structure of YbtPQ importer== | |||
<StructureSection load='6p6i' size='340' side='right'caption='[[6p6i]], [[Resolution|resolution]] 3.67Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6p6i]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6P6I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6P6I FirstGlance]. <br> | |||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6p6i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6p6i OCA], [http://pdbe.org/6p6i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6p6i RCSB], [http://www.ebi.ac.uk/pdbsum/6p6i PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6p6i ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
To fight for essential metal ions, human pathogens secrete virulence-associated siderophores and retake the metal-chelated siderophores through a subfamily of adenosine triphosphate (ATP)-binding cassette (ABC) importer, whose molecular mechanisms are completely unknown. We have determined multiple structures of the yersiniabactin importer YbtPQ from uropathogenic Escherichia coli (UPEC) at inward-open conformation in both apo and substrate-bound states by cryo-electron microscopy. YbtPQ does not adopt any known fold of ABC importers but surprisingly adopts the fold of type IV ABC exporters. To our knowledge, it is the first time an exporter fold of ABC importer has been reported. We have also observed two unique features in YbtPQ: unwinding of a transmembrane helix in YbtP upon substrate release and tightly associated nucleotide-binding domains without bound nucleotides. Together, our study suggests that siderophore ABC importers have a distinct transport mechanism and should be classified as a separate subfamily of ABC importers. | |||
Pathogenic siderophore ABC importer YbtPQ adopts a surprising fold of exporter.,Wang Z, Hu W, Zheng H Sci Adv. 2020 Feb 5;6(6):eaay7997. doi: 10.1126/sciadv.aay7997. eCollection 2020 , Feb. PMID:32076651<ref>PMID:32076651</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6p6i" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Hu, W]] | |||
[[Category: Wang, Z]] | |||
[[Category: Zheng, H]] | |||
[[Category: Abc importer]] | |||
[[Category: Transport protein]] | |||
[[Category: Yersiniabactin]] | |||
