Crystal structure of bacterial haem importer complex in the inward-facing conformation-Reference-Cited by-同舟云学术

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Crystal structure of bacterial haem importer complex in the inward-facing conformation

Published:2016-11-10 Issue:1 Volume:7 Page:
ISSN:2041-1723
Container-title:Nature Communications
language:en
Short-container-title:Nat Commun

Author:

Naoe Youichi,Nakamura Nozomi,Doi Akihiro,Sawabe Mia,Nakamura Hiro,Shiro Yoshitsugu,Sugimoto Hiroshi

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/ncomms13411.pdf

Reference37 articles.

1. Thompson, J. M., Jones, H. A. & Perry, R. D. Molecular characterization of the hemin uptake locus (hmu) from Yersinia pestis and analysis of hmu mutants for hemin and hemoprotein utilization. Infect. Immun. 67, 3879–3892 (1999).

2. Hornung, J. M., Jones, H. A. & Perry, R. D. The hmu locus of Yersinia pestis is essential for utilization of free haemin and haem-protein complexes as iron sources. Mol. Microbiol. 20, 725–739 (1996).

3. Woo, J. S., Zeltina, A., Goetz, B. A. & Locher, K. P. X-ray structure of the Yersinia pestis heme transporter HmuUV. Nat. Struct. Mol. Biol. 19, 1310–1315 (2012).

4. Pinkett, H. W., Lee, A. T., Lum, P., Locher, K. P. & Rees, D. C. An inward-facing conformation of a putative metal-chelate-type ABC transporter. Science 315, 373–377 (2007).

5. Korkhov, V. M., Mireku, S. A., Veprintsev, D. B. & Locher, K. P. Structure of AMP-PNP-bound BtuCD and mechanism of ATP-powered vitamin B12 transport by BtuCD-F. Nat. Struct. Mol. Biol. 21, 1097–1099 (2014).

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