Ontology highlight
ABSTRACT:
SUBMITTER: Suits MD
PROVIDER: S-EPMC1287972 | biostudies-literature | 2005 Nov
REPOSITORIES: biostudies-literature
Suits Michael D L MD Pal Gour P GP Nakatsu Kanji K Matte Allan A Cygler Miroslaw M Jia Zongchao Z
Proceedings of the National Academy of Sciences of the United States of America 20051107 47
Heme oxygenases (HOs) catalyze the oxidation of heme to biliverdin, carbon monoxide (CO), and free iron. Iron acquisition is critical for invading microorganisms to enable survival and growth. Here we report the crystal structure of ChuS, which displays a previously uncharacterized fold and is unique compared with other characterized HOs. Despite only 19% sequence identity between the N- and C-terminal halves, these segments of ChuS represent a structural duplication, with a root-mean-square dev ...[more]