The Single-domain Globin from the Pathogenic Bacterium Campylobacter jejuni: NOVEL D-HELIX CONFORMATION, PROXIMAL HYDROGEN BONDING THAT INFLUENCES LIGAND BINDING, AND PEROXIDASE-LIKE REDOX PROPERTIES

The food-borne pathogen Campylobacter jejuni possesses a single-domain globin (Cgb) whose role in detoxifying nitric oxide has been unequivocally demonstrated through genetic and molecular approaches. The x-ray structure of cyanide-bound Cgb has been solved to a resolution of 1.35 Å. The overall fol...

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Hlavní autoři: Shepherd, Mark, Barynin, Vladimir, Lu, Changyuan, Bernhardt, Paul V., Wu, Guanghui, Yeh, Syun-Ru, Egawa, Tsuyoshi, Sedelnikova, Svetlana E., Rice, David W., Wilson, Jayne Louise, Poole, Robert K.
Médium: Artigo
Jazyk:Inglês
Vydáno: American Society for Biochemistry and Molecular Biology 2010
Témata:
Protein Structure and Folding
On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC2857070/
https://ncbi.nlm.nih.gov/pubmed/20164176
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M109.084509
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