A shape-shifting redox foldase contributes to Proteus mirabilis copper resistance-Reference-Cited by-同舟云学术

A shape-shifting redox foldase contributes to Proteus mirabilis copper resistance

Published:2017-07-19 Issue:1 Volume:8 Page:
ISSN:2041-1723
Container-title:Nature Communications
language:en
Short-container-title:Nat Commun

Author:

Furlong Emily J.,Lo Alvin W.,Kurth Fabian,Premkumar Lakshmanane,Totsika Makrina^ORCID,Achard Maud E. S.,Halili Maria A.,Heras Begoña,Whitten Andrew E.,Choudhury Hassanul G.,Schembri Mark A.,Martin Jennifer L.^ORCID

Publisher

Springer Science and Business Media LLC

Subject

General Physics and Astronomy,General Biochemistry, Genetics and Molecular Biology,General Chemistry

Link

http://www.nature.com/articles/ncomms16065.pdf

Reference58 articles.

1. Martin, J. L., Bardwell, J. C. & Kuriyan, J. Crystal structure of the DsbA protein required for disulfide bond formation in vivo. Nature 365, 464–468 (1993).

2. Inaba, K. et al. Crystal structure of the DsbB-DsbA complex reveals a mechanism of disulfide bond generation. Cell 127, 789–801 (2006).

3. McCarthy, A. A. et al. Crystal structure of the protein disulfide isomerase, DsbC, from Escherichia coli. Nat. Struct. Biol. 7, 196–199 (2000).

4. Missiakas, D., Georgopoulos, C. & Raina, S. The Escherichia coli dsbC (xprA) gene encodes a periplasmic protein involved in disulfide bond formation. EMBO J. 13, 2013–2020 (1994).

5. Heras, B., Edeling, M. A., Schirra, H. J., Raina, S. & Martin, J. L. Crystal structures of the DsbG disulfide isomerase reveal an unstable disulfide. Proc. Natl Acad. Sci. USA 101, 8876–8881 (2004).

Cited by 23 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Scs system links copper and redox homeostasis in bacterial pathogens;Journal of Biological Chemistry;2024-03

2. Bacterial suppressor-of-copper-sensitivity (Scs) proteins exhibit diverse thiol-disulfide oxidoreductase cellular functions;2023-02-07

3. Ucl fimbriae regulation and glycan receptor specificity contribute to gut colonisation by extra-intestinal pathogenic Escherichia coli;PLOS Pathogens;2022-06-14

4. Expression, purification and characterization of the suppressor of copper sensitivity (Scs) B membrane protein from Proteus mirabilis;Protein Expression and Purification;2022-05

5. The suppressor of copper sensitivity protein C from Caulobacter crescentus is a trimeric disulfide isomerase that binds copper(I) with subpicomolar affinity;Acta Crystallographica Section D Structural Biology;2022-02-21