X-RAY CRYSTALLOGRAPHIC DETERMINATION OF A COLLAGEN-LIKE PEPTIDE WITH THE REPEATING SEQUENCE (PRO-PRO-GLY)

Citation
Rz. Kramer et al., X-RAY CRYSTALLOGRAPHIC DETERMINATION OF A COLLAGEN-LIKE PEPTIDE WITH THE REPEATING SEQUENCE (PRO-PRO-GLY), Journal of Molecular Biology, 280(4), 1998, pp. 623-638
Citations number
30
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Biology
ISSN journal
0022-2836
Volume
280
Issue
4
Year of publication
1998
Pages
623 - 638
Database
ISI
SICI code
0022-2836(1998)280:4<623:XCDOAC>2.0.ZU;2-G
Abstract
The crystal structure of the triple-helical peptide (Pro-Pro-Gly)(10) has been re-determined to obtain a more accurate description for this widely studied collagen model and to pros ide a comparison with the re cent high-resolution crystal structure of a collagen-like peptide cont aining Pro-Hyp-Gly regions. This structure demonstrated that hydroxypr oline participates extensively In a repetitive hydrogen-bonded assembl y between the peptide and the solvent molecules. Two separate structur al studies of the peptide (Pro-Pro-Gly)(10) were performed with differ ent crystallization conditions, data collection temperatures, and X-ra y sources. The polymer like structure of one triple-helical repeat of Pro-Pro-Gly has been determined to 2.0 Angstrom resolution in one case and 1.7 Angstrom resolution in the other. The solvent structures of t he two peptides were independently determined specifically for validat ion purposes. The two structures display a reverse chain trace compare d with the original structure determination. In comparison with the Hy p-containing peptide, the two Pro-Pro-Gly structures demonstrate very similar molecular conformation and analogous hydration patterns involv ing carbonyl groups, but have different crystal packing. This differen ce in crystal packing indicates that the involvement of hydroxyproline in an extended hydration network is critical for the lateral assembly and supermolecular structure of collagen. (C) 1998 Academic Press.