Work

Expression, purification, crystallization and preliminary X-ray studies of a prolyl-4-hydroxylase protein fromBacillus anthracis

Year: 2008

Type: article

Abstract: 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 A resolution.

Source: Acta Crystallographica Section F Structural Biology and Crystallization Communications

DOI: 10.1107/s1744309108023439

Authors: Megen A. Miller, Emily E. Scott, Julian Limburg

Institution: University of Kansas

Language: English

Topic: Enzyme Structure and Function

Subfield: Structural Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funders: National Institute of General Medical Sciences, National Center for Research Resources

Awards: G5686254363, Protein Structure and Function, Training Grant in Dynamic Aspects of Chemical Biology, Mechanism and inhibition of collagen prolyl-4-hydroxylases