Ontology highlight
ABSTRACT:
SUBMITTER: Watanabe M
PROVIDER: S-EPMC2661414 | biostudies-literature | 2008 Oct
REPOSITORIES: biostudies-literature
Watanabe Masato M Tanaka Yoshikazu Y Suenaga Ayuko A Kuroda Makoto M Yao Min M Watanabe Nobuhisa N Arisaka Fumio F Ohta Toshiko T Tanaka Isao I Tsumoto Kouhei K
The Journal of biological chemistry 20080730 42
To elucidate the heme acquisition system in pathogenic bacteria, we investigated the heme-binding properties of the third NEAT domain of IsdH (IsdH-NEAT3), a receptor for heme located on the surfaces of pathogenic bacterial cells, by using x-ray crystallography, isothermal titration calorimetry, examination of absorbance spectra, mutation analysis, size-exclusion chromatography, and analytical ultracentrifugation. We found the following: 1) IsdH-NEAT3 can bind with multiple heme molecules by two ...[more]