Expression, purification, crystallization and preliminary X‐ray studies of a prolyl‐4‐hydroxylase protein from Bacillus anthracis
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 selenomethionine‐labeled anthrax‐P4H recombinantly expressed in Escherichia coli have been collected to 1.4 Å resolution.
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