Crystal structure analysis of collagen model peptide (Pro-pro-Gly)10.
Single crystals of (Pro-Pro-Gly)10 were grown by the hanging drop method. The crystals diffracted to a resolution of 1.8 A. In the crystals the polypeptides form triple helices that aggregate end-to-end mediated by the solvent molecules, with the basic repeat being 20 A along the helical axis. Analysis of the 20 A structure of (Pro-Pro-Gly)10 using data up to a resolution of 1.9 A revealed that the overall structure is in accordance with the 7/2 model proposed for collagen. The three strands are held together by the (Gly) N-H O (Pro-X) hydrogen bond interactions, and additional stability is provided by the (Pro-Y) Calpha -H O (Pro-X) hydrogen bonding interactions.
Nagarajan
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V
Department of Biotechnology and Life Science, Faculty of Technology, Tokyo University of Agriculture and Technology, Naka-cho, Koganei-shi, Tokyo, 184-8588, Japan.
Kamitori
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S
Okuyama
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K
D003094:Collagen / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D006860:Hydrogen Bonding; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation; D014867:Water
D010455:Peptides; D014867:Water; D003094:Collagen