Ontology highlight
ABSTRACT:
SUBMITTER: Miller MA
PROVIDER: S-EPMC2531266 | biostudies-literature | 2008 Sep
REPOSITORIES: biostudies-literature
Miller Megen A MA Scott Emily E EE Limburg Julian J
Acta crystallographica. Section F, Structural biology and crystallization communications 20080809 Pt 9
Collagen prolyl-4-hydroxylase (C-P4H) catalyzes the hydroxylation of specific proline residues in procollagen, which is an essential step in collagen biosynthesis. A new form of P4H from Bacillus anthracis (anthrax-P4H) that shares many characteristics with the type I C-P4H from human has recently been characterized. The structure of anthrax-P4H could provide important insight into the chemistry of C-P4Hs and into the function of this unique homodimeric P4H. X-ray diffraction data of selenomethi ...[more]