2cuo
From Proteopedia
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[[Image:2cuo.gif|left|200px]] | [[Image:2cuo.gif|left|200px]] | ||
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'''Collagen model peptide (PRO-PRO-GLY)9''' | '''Collagen model peptide (PRO-PRO-GLY)9''' | ||
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==About this Structure== | ==About this Structure== | ||
| - | + | Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CUO OCA]. | |
==Reference== | ==Reference== | ||
Repetitive interactions observed in the crystal structure of a collagen-model peptide, [(Pro-Pro-Gly)9]3., Hongo C, Noguchi K, Okuyama K, Tanaka Y, Nishino N, J Biochem. 2005 Aug;138(2):135-44. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16091587 16091587] | Repetitive interactions observed in the crystal structure of a collagen-model peptide, [(Pro-Pro-Gly)9]3., Hongo C, Noguchi K, Okuyama K, Tanaka Y, Nishino N, J Biochem. 2005 Aug;138(2):135-44. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16091587 16091587] | ||
| - | [[Category: Protein complex]] | ||
[[Category: Hongo, C.]] | [[Category: Hongo, C.]] | ||
[[Category: Nishino, N.]] | [[Category: Nishino, N.]] | ||
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[[Category: Okuyama, K.]] | [[Category: Okuyama, K.]] | ||
[[Category: Tanaka, Y.]] | [[Category: Tanaka, Y.]] | ||
| - | [[Category: | + | [[Category: Collagen model peptide]] |
| - | [[Category: | + | [[Category: Puckering]] |
| - | [[Category: | + | [[Category: Triple-helix]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 23:06:40 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 20:06, 3 May 2008
Collagen model peptide (PRO-PRO-GLY)9
Overview
The crystal structure of a collagen-model peptide [(Pro-Pro-Gly)(9)](3) has been determined at 1.33 A resolution. Diffraction data were collected at 100 K using synchrotron radiation, which led to the first structural study of [(Pro-Pro-Gly)(n)](3) under cryogenic conditions. The crystals belong to the P2(1) space group with cell parameters of a = 25.95, b = 26.56, c = 80.14 Angstroms and beta = 90.0 degrees. The overall molecular conformation was consistent with the left-handed 7/2-helical model with an axial repeat of 20 A for native collagen. A total of 332 water molecules were found in an asymmetric unit. Proline residues in adjacent triple-helices exhibited three types of hydrophobic interactions. Furthermore, three types of hydrogen-bonding networks mediated by water molecules were observed between adjacent triple-helices. These hydrophobic interactions and hydrogen-bonding networks occurred at intervals of 20 Angstroms along the c-axis based on the previous sub-cell structures [(Pro-Pro-Gly)(n)](3) (n = 9, 10), which were also seen in the full-cell structure of [(Pro-Pro-Gly)(10)](3). Five proline residues at the Y position in the X-Y-Gly triplet were found in a down-puckering conformation, this being inconsistent with the recently proposed propensity-based hypothesis. These proline residues were forced to adopt opposing puckering because of the prevailing hydrophobic interaction between triple-helices compared with the Pro:Pro stacking interaction within a triple-helix.
About this Structure
Full crystallographic information is available from OCA.
Reference
Repetitive interactions observed in the crystal structure of a collagen-model peptide, [(Pro-Pro-Gly)9]3., Hongo C, Noguchi K, Okuyama K, Tanaka Y, Nishino N, J Biochem. 2005 Aug;138(2):135-44. PMID:16091587 Page seeded by OCA on Sat May 3 23:06:40 2008
