Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

6PSN

Anthrax toxin protective antigen channels bound to lethal factor

Summary for 6PSN
Entry DOI10.2210/pdb6psn/pdb
EMDB information20459
DescriptorProtective antigen, Lethal factor, CALCIUM ION (3 entities in total)
Functional Keywordstranslocase, anthrax toxin, protective antigen, lethal factor
Biological sourceBacillus anthracis
More
Total number of polymer chains8
Total formula weight539101.86
Authors
Hardenbrook, N.J.,Liu, S.,Zhou, K.,Zhou, Z.H.,Krantz, B.A. (deposition date: 2019-07-12, release date: 2020-03-04, Last modification date: 2024-03-20)
Primary citationHardenbrook, N.J.,Liu, S.,Zhou, K.,Ghosal, K.,Hong Zhou, Z.,Krantz, B.A.
Atomic structures of anthrax toxin protective antigen channels bound to partially unfolded lethal and edema factors.
Nat Commun, 11:840-840, 2020
Cited by
PubMed Abstract: Following assembly, the anthrax protective antigen (PA) forms an oligomeric translocon that unfolds and translocates either its lethal factor (LF) or edema factor (EF) into the host cell. Here, we report the cryo-EM structures of heptameric PA channels with partially unfolded LF and EF at 4.6 and 3.1-Å resolution, respectively. The first α helix and β strand of LF and EF unfold and dock into a deep amphipathic cleft, called the α clamp, which resides at the interface of two PA monomers. The α-clamp-helix interactions exhibit structural plasticity when comparing the structures of lethal and edema toxins. EF undergoes a largescale conformational rearrangement when forming the complex with the channel. A critical loop in the PA binding interface is displaced for about 4 Å, leading to the weakening of the binding interface prior to translocation. These structures provide key insights into the molecular mechanisms of translocation-coupled protein unfolding and translocation.
PubMed: 32047164
DOI: 10.1038/s41467-020-14658-6
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (4.6 Å)
Structure validation

238268

数据于2025-07-02公开中

PDB statisticsPDBj update infoContact PDBjnumon