6P6J

Structure of YbtPQ importer with substrate Ybt-Fe bound

Summary for 6P6J

• Entry DOI: 10.2210/pdb6p6j/pdb
• EMDB information: 20262 20263 20264
• Descriptor: inner membrane ABC-transporter, ABC transporter protein, yersiniabactin, ... (4 entities in total)
• Functional Keywords: abc importer, yersiniabactin, transport protein
• Biological source: Escherichia coli (strain UTI89 / UPEC); More
• Total number of polymer chains: 2
• Total formula weight: 133345.14

Authors

Wang, Z.,Hu, W.,Zheng, H. (deposition date: 2019-06-04, release date: 2020-03-04, Last modification date: 2024-03-13)

Primary citation

Wang, Z.,Hu, W.,Zheng, H.
Pathogenic siderophore ABC importer YbtPQ adopts a surprising fold of exporter.
Sci Adv, 6:eaay7997-eaay7997, 2020

PubMed Abstract: 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 (UPEC) at inward-open conformation in both 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.

PubMed: 32076651
DOI: 10.1126/sciadv.aay7997

Experimental method

ELECTRON MICROSCOPY (3.4 Å)