Issue 52, 2012
From the journal:

Chemical Communications

Structural basis for oxygen sensing and signal transduction of the heme-based sensor protein Aer2 from Pseudomonas aeruginosa†‡

Hitomi Sawai,a   Hiroshi Sugimoto,*b   Yoshitsugu Shiro,b   Haruto Ishikawa,c   Yasuhisa Mizutanic  and  Shigetoshi Aono*a  

* Corresponding authors

a Okazaki Institute for Integrative Bioscience, National Institutes of Natural Sciences, 5-1 Higashiyama, Myodaiji, Okazaki 444-8787, Japan
E-mail: aono@ims.ac.jp
Fax: +81-564-59-5576
Tel: +81-564-59-5575

b RIKEN SPring-8 Center, Harima Institute, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5148, Japan
E-mail: sugimoto@spring8.or.jp
Fax: +81-791-58-2818
Tel: +81-791-58-2817

c Department of Chemistry, Graduate School of Science, Osaka University, 1-1 Machikaneyama, Toyonaka, Osaka 560-0043, Japan

Abstract

The crystal structure of a truncated Aer2, a signal transducer protein from Pseudomonas aeruginosa, consisting of the heme-containing PAS and di-HAMP domains revealed that a distal tryptophan residue (Trp283) plays an important role in stabilizing the heme-bound O2 and intra-molecular signal transduction upon O2 binding.

Graphical abstract: Structural basis for oxygen sensing and signal transduction of the heme-based sensor protein Aer2 from Pseudomonas aeruginosa

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Article information

DOI
https://doi.org/10.1039/C2CC32549G
Article type
Communication
Submitted
06 Feb 2012
Accepted
08 May 2012
First published
09 May 2012

Chem. Commun., 2012,48, 6523-6525

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Structural basis for oxygen sensing and signal transduction of the heme-based sensor protein Aer2 from Pseudomonas aeruginosa

H. Sawai, H. Sugimoto, Y. Shiro, H. Ishikawa, Y. Mizutani and S. Aono, Chem. Commun., 2012, 48, 6523 DOI: 10.1039/C2CC32549G

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