Zobrazeno 1 - 10
of 23
pro vyhledávání: '"Paul K. Kienker"'
Publikováno v:
The Journal of General Physiology
Cysteine substitution accessibility analysis suggests that the TH6–TH7 segment forms a constriction in the diphtheria toxin T-domain channel.
Low pH triggers the translocation domain of diphtheria toxin (T-domain), which contains 10 α helices
Low pH triggers the translocation domain of diphtheria toxin (T-domain), which contains 10 α helices
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::58e2567ce69d8e58144e2270bbe73b02
https://doi.org/10.1085/jgp.201411326
https://doi.org/10.1085/jgp.201411326
Publikováno v:
The Journal of General Physiology
Anthrax toxin is composed of three proteins: a translocase heptameric channel, (PA(63))(7), formed from protective antigen (PA), which allows the other two proteins, lethal factor (LF) and edema factor (EF), to translocate across a host cell's endoso
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f8f0e95abad357f6ef2104193ad7ce19
https://doi.org/10.1085/jgp.201110627
https://doi.org/10.1085/jgp.201110627
Publikováno v:
The Journal of General Physiology
Colicin Ia is a bactericidal protein of 626 amino acid residues that kills its target cell by forming a channel in the inner membrane; it can also form voltage-dependent channels in planar lipid bilayer membranes. The channel-forming activity resides
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c0a2ca1d8c26d6855264736909844e64
https://doi.org/10.1085/jgp.200810042
https://doi.org/10.1085/jgp.200810042
Publikováno v:
Biochemistry. 47:1778-1788
Some of the bactericidal proteins known as colicins exert their toxic action by forming a large, nonselective channel in the inner membrane of target bacteria. The structure of this channel is unknown. It conducts large ions but has a much smaller co
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::07250c14e3153e4cc253a0e30df2261f
https://doi.org/10.1021/bi701900x
https://doi.org/10.1021/bi701900x
Structure of colicin I receptor bound to the R-domain of colicin Ia: implications for protein import
Autor:
Paul K. Kienker, Lothar Esser, Petra Lukacik, Travis J. Barnard, Susan K. Buchanan, Sylvestre Grizot, Rodolfo Ghirlando, Karen S. Jakes, Maruf M.U. Ali
Publikováno v:
The EMBO Journal. 26:2594-2604
Colicin Ia is a 69 kDa protein that kills susceptible Escherichia coli cells by binding to a specific receptor in the outer membrane, colicin I receptor (70 kDa), and subsequently translocating its channel forming domain across the periplasmic space,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aeaa5852b09faf037c16bd4bf7dbfe66
https://doi.org/10.1038/sj.emboj.7601693
https://doi.org/10.1038/sj.emboj.7601693
Publikováno v:
The Journal of membrane biology. 249(1-2)
The translocation domain (T-domain) of diphtheria toxin contains 10 α helices in the aqueous crystal structure. Upon exposure to a planar lipid bilayer under acidic conditions, it inserts to form a channel and transport the attached amino-terminal c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a6ad146374cac009621c8973f001c18f
https://pubmed.ncbi.nlm.nih.gov/26645703
https://pubmed.ncbi.nlm.nih.gov/26645703
Publikováno v:
The Journal of General Physiology
The bacterial toxin colicin Ia forms voltage-gated channels in planar lipid bilayers. The toxin consists of three domains, with the carboxy-terminal domain (C-domain) responsible for channel formation. The C-domain contributes four membrane-spanning
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e3f3d16a2fa869b5d1600e0861177a13
http://europepmc.org/articles/PMC2229546
http://europepmc.org/articles/PMC2229546
Publikováno v:
The Journal of General Physiology
Colicin Ia, a 626-residue bactericidal protein, consists of three domains, with the carboxy-terminal domain (C domain) responsible for channel formation. Whole colicin Ia or C domain added to a planar lipid bilayer membrane forms voltage-gated channe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7c06eea25236e5073581fdbe2c350ae0
https://doi.org/10.1085/jgp.116.4.587
https://doi.org/10.1085/jgp.116.4.587
Publikováno v:
Journal of Membrane Biology. 157:27-37
Colicin Ia is a bactericidal protein that forms voltage-dependent, ion-conducting channels, both in the inner membrane of target bacteria and in planar bilayer membranes. Its amino acid sequence is rich in charged residues, except for a hydrophobic s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6f44f5275eccf3eeb80286e9f158dab1
https://doi.org/10.1007/s002329900213
https://doi.org/10.1007/s002329900213
Autor:
Alexey S. Ladokhin, Mauricio Vargas-Uribe, Alan Finkelstein, Mykola V. Rodnin, Paul K. Kienker
Publikováno v:
Biochemistry. 52(20)
The translocation (T) domain plays a key role in the entry of diphtheria toxin into the cell. Upon endosomal acidification, the T-domain undergoes a series of conformational changes that lead to its membrane insertion and formation of a channel. Rece
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::39b2b5345bec75fc5dd85818ec8e06eb
https://pubmed.ncbi.nlm.nih.gov/23621842
https://pubmed.ncbi.nlm.nih.gov/23621842