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''' | + | {{Structure |
| + | |PDB= 2cuo |SIZE=350|CAPTION= <scene name='initialview01'>2cuo</scene>, resolution 1.33Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''Collagen model peptide (PRO-PRO-GLY)9''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2CUO is a [ | + | 2CUO is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/ ]. 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:// | + | 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: Protein complex]] | ||
[[Category: Hongo, C.]] | [[Category: Hongo, C.]] | ||
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[[Category: triple-helix]] | [[Category: triple-helix]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:20:07 2008'' |
Revision as of 14:20, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
2CUO is a Protein complex structure of sequences from [1]. 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
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