1K6F

Crystal Structure of the Collagen Triple Helix Model [(Pro-Pro-Gly)10]3

Summary for 1K6F

• Entry DOI: 10.2210/pdb1k6f/pdb
• Descriptor: collagen triple helix (2 entities in total)
• Functional Keywords: collagen stability, puckering, amino acid preferences, triple helix, structural protein
• Total number of polymer chains: 6
• Total formula weight: 15184.97

Authors

Berisio, R.,Vitagliano, L.,Mazzarella, L.,Zagari, A. (deposition date: 2001-10-16, release date: 2002-01-30, Last modification date: 2024-02-07)

Primary citation

Berisio, R.,Vitagliano, L.,Mazzarella, L.,Zagari, A.
Crystal structure of the collagen triple helix model [(Pro-Pro-Gly)(10)](3)
Protein Sci., 11:262-270, 2002

PubMed Abstract: The first report of the full-length structure of the collagen-like polypeptide [(Pro-Pro-Gly)(10)](3) is given. This structure was obtained from crystals grown in a microgravity environment, which diffracted up to 1.3 A, using synchrotron radiation. The final model, which was refined to an R(factor) of 0.18, is the highest-resolution description of a collagen triple helix reported to date. This structure provides clues regarding a series of aspects related to collagen triple helix structure and assembly. The strict dependence of proline puckering on the position inside the Pro-Pro-Gly triplets and the correlation between backbone and side chain dihedral angles support the propensity-based mechanism of triple helix stabilization/destabilization induced by hydroxyproline. Furthermore, the analysis of [(Pro-Pro-Gly)(10)](3) packing, which is governed by electrostatic interactions, suggests that charges may act as locking features in the axial organization of triple helices in the collagen fibrils.

PubMed: 11790836
DOI: 10.1110/ps.32602

Experimental method

X-RAY DIFFRACTION (1.3 Å)