Crystallization of the proline-rich-peptide binding domain of human type I collagen prolyl 4-hydroxylase.
Collagen prolyl 4-hydroxylases catalyze the hydroxylation of -X-Pro-Gly- sequences and play an essential role in the synthesis of all collagens. They require Fe(2+), 2-oxoglutarate, molecular oxygen and ascorbate, and all vertebrate collagen prolyl 4-hydroxylases are alpha(2)beta(2) tetramers. The alpha-subunits contain separate catalytic and peptide substrate-binding domains. Here, the crystallization of the peptide substrate-binding domain consisting of residues 144-244 of the 517-residue human alpha(I) subunit is described. The crystals are well ordered and diffract to at least 3 A. The space group is P3(1) or P3(2) and the asymmetric unit most probably contains a dimer.
Pekkala
Mira
M
Biocenter Oulu and Department of Biochemistry, University of Oulu, PO Box 3000, FIN-90014, Finland.
Hieta
Reija
R
Kursula
Petri
P
Kivirikko
Kari I
KI
Wierenga
Rik K
RK
Myllyharju
Johanna
J
D024042:Collagen Type I / Q000378:metabolism*; D003460:Crystallization; D006801:Humans; D010455:Peptides / Q000737:chemistry / Q000378:metabolism; D011393:Procollagen-Proline Dioxygenase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D011392:Proline / Q000737:chemistry*; D017434:Protein Structure, Tertiary; D021122:Protein Subunits / Q000737:chemistry; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D014961:X-Ray Diffraction
D024042:Collagen Type I; D010455:Peptides; D021122:Protein Subunits; D011994:Recombinant Proteins; D011392:Proline; D011393:Procollagen-Proline Dioxygenase