Zobrazeno 1 - 10
of 53
pro vyhledávání: '"Vladimir N. Kasho"'
Autor:
Els Pardon, H. Ronald Kaback, Robert M. Stroud, Vladimir N. Kasho, Hemant Kumar, Janet Finer-Moore, Irina Smirnova, Jan Steyaert
Publikováno v:
PloS one, vol 15, iss 5
PLoS ONE, Vol 15, Iss 5, p e0232846 (2020)
PLoS ONE
PLoS ONE, Vol 15, Iss 5, p e0232846 (2020)
PLoS ONE
Funder: research foundation-flanders
The structure of lactose permease, stabilized in a periplasmic open conformation by two Gly to Trp replacements (LacYww) and complexed with a nanobody directed against this conformation, provides the highest
The structure of lactose permease, stabilized in a periplasmic open conformation by two Gly to Trp replacements (LacYww) and complexed with a nanobody directed against this conformation, provides the highest
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d5b32a2fde5658007e7e83fbed41f0c4
https://escholarship.org/uc/item/36t656kj
https://escholarship.org/uc/item/36t656kj
Autor:
Irina Smirnova, H. Ronald Kaback, Xiaoxu Jiang, Els Pardon, Robert M. Stroud, Jan Steyaert, Vladimir N. Kasho, Janet Finer-Moore, Hemant Kumar
Publikováno v:
Proceedings of the National Academy of Sciences. 115:8769-8774
The lactose permease of Escherichia coli (LacY), a dynamic polytopic membrane transport protein, catalyzes galactoside/H(+) symport and operates by an alternating access mechanism that exhibits multiple conformations, the distribution of which is alt
Autor:
Stephen G. Withers, H. Ronald Kaback, Hong-Ming Chen, Xiaoxu Jiang, Irina Smirnova, Vladimir N. Kasho
Publikováno v:
Proceedings of the National Academy of Sciences. 115:4146-4151
Binding kinetics of α-galactopyranoside homologs with fluorescent aglycones of different sizes and shapes were determined with the lactose permease (LacY) of Escherichia coli by FRET from Trp151 in the binding site of LacY to the fluorophores. Fast
Publikováno v:
Biochemistry. 56:1943-1950
Galactoside/H+ symport by the lactose permease of Escherichia coli (LacY) involves reciprocal opening and closing of periplasmic and cytoplasmic cavities so that sugar- and H+-binding sites become alternatively accessible to either side of the membra
Autor:
H. Ronald Kaback, Els Pardon, Vladimir N. Kasho, Nieng Yan, Meng Ke, Jianping Wu, Kunio Hirata, Irina Smirnova, Xin Jiang, Jan Steyaert
Publikováno v:
Proceedings of the National Academy of Sciences. 113:12420-12425
The lactose permease of Escherichia coli (LacY), a dynamic polytopic membrane protein, catalyzes galactoside-H(+) symport and operates by an alternating access mechanism that exhibits multiple conformations, the distribution of which is altered by su
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 115(50)
The lactose permease of Escherichia coli (LacY) utilizes an alternating access symport mechanism with multiple conformational intermediates, but only inward (cytoplasmic)- or outward (periplasmic)-open structures have been characterized by X-ray crys
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America, vol 111, iss 52
Smirnova, I; Kasho, V; Jiang, X; Pardon, E; Steyaert, J; & Kaback, HR. (2014). Outward-facing conformers of LacY stabilized by nanobodies. Proceedings of the National Academy of Sciences of the United States of America, 111(52), 18548-18553. doi: 10.1073/pnas.1422265112. UCLA: Retrieved from: http://www.escholarship.org/uc/item/0rw9g49d
Smirnova, I; Kasho, V; Jiang, X; Pardon, E; Steyaert, J; & Kaback, HR. (2014). Outward-facing conformers of LacY stabilized by nanobodies. Proceedings of the National Academy of Sciences of the United States of America, 111(52), 18548-18553. doi: 10.1073/pnas.1422265112. UCLA: Retrieved from: http://www.escholarship.org/uc/item/0rw9g49d
© 2014, National Academy of Sciences. All rights reserved. The lactose permease of Escherichia coli (LacY), a highly dynamic polytopic membrane protein, catalyzes stoichiometric galactoside/H+symport by an alternating access mechanism and exhibits m
Autor:
H. Ronald Kaback, Robert M. Stroud, Irina Smirnova, Vladimir N. Kasho, Hemant Kumar, Janet Finer-Moore
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America, vol 111, iss 5
Kumar, H; Kasho, V; Smirnova, I; Finer-Moore, JS; Kaback, HR; & Stroud, RM. (2014). Structure of sugar-bound LacY. Proceedings of the National Academy of Sciences of the United States of America, 111(5), 1784-1788. doi: 10.1073/pnas.1324141111. UCLA: Retrieved from: http://www.escholarship.org/uc/item/52x4z6q2
Kumar, H; Kasho, V; Smirnova, I; Finer-Moore, JS; Kaback, HR; & Stroud, RM. (2014). Structure of sugar-bound LacY. Proceedings of the National Academy of Sciences of the United States of America, 111(5), 1784-1788. doi: 10.1073/pnas.1324141111. UCLA: Retrieved from: http://www.escholarship.org/uc/item/52x4z6q2
Here we describe the X-ray crystal structure of a double-Trp mutant (Gly46→Trp/Gly262→Trp) of the lactose permease of Escherichia coli (LacY) with a bound, high-affinity lactose analog. Although thought to be arrested in an open-outward conformat
The lactose permease of Escherichia coli (LacY), a highly dynamic membrane protein, catalyzes symport of a galactopyranoside and an H(+) by using an alternating access mechanism, and the transport cycle involves multiple conformational states. Single
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fed97cbd155febfdc8ffb659f71f3184
https://europepmc.org/articles/PMC4653160/
https://europepmc.org/articles/PMC4653160/
Publikováno v:
Biochemistry. 50:9684-9693
Crystal structures of the lactose permease of Escherichia coli (LacY) reveal 12, mostly irregular transmembrane α-helices surrounding a large cavity open to the cytoplasm and a tightly sealed periplasmic side (inward-facing conformation) with the su