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PDBsum entry 1k6f
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Structural protein
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PDB id
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1k6f
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References listed in PDB file
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Key reference
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Title
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Crystal structure of the collagen triple helix model [(pro-Pro-Gly)(10)](3).
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Authors
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R.Berisio,
L.Vitagliano,
L.Mazzarella,
A.Zagari.
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Ref.
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Protein Sci, 2002,
11,
262-270.
[DOI no: ]
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PubMed id
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Abstract
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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.
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Figure 1.
Fig. 1. (A) Organization of the [(Pro-Pro-Gly)[10][3]
triple helices in the ac plane. Chains are colored with a
ramping code from blue (N-termini) to red (C-termini). The two
molecules in the asymmetric unit are the top-center (molecule 1)
and the bottom-center (molecule 2) molecules. (B) Average model
obtained in the subcell approximation (Vitagliano et al. 2001a)
in the ac` plane. The c` corresponds to a ninth of the
full-length c axis. (C) Electron density map (2Fo-Fc), extended
to the whole unit cell, contoured at 2.0  . (D) Omit
map (Fo-Fc) of a representative triplet contoured at 3.5 .
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Figure 3.
Fig. 3. Distribution of water molecules as a function of
their distance from the nearest protein atom.
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The above figures are
reprinted
by permission from the Protein Society:
Protein Sci
(2002,
11,
262-270)
copyright 2002.
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Secondary reference #1
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Title
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Preferred proline puckerings in cis and trans peptide groups: implications for collagen stability.
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Authors
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L.Vitagliano,
R.Berisio,
A.Mastrangelo,
L.Mazzarella,
A.Zagari.
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Ref.
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Protein Sci, 2001,
10,
2627-2632.
[DOI no: ]
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PubMed id
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Secondary reference #2
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Title
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Structural bases of collagen stabilization induced by proline hydroxylation.
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Authors
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L.Vitagliano,
R.Berisio,
L.Mazzarella,
A.Zagari.
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Ref.
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Biopolymers, 2001,
58,
459-464.
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PubMed id
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Secondary reference #3
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Title
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Crystal structure of a collagen-Like polypeptide with repeating sequence pro-Hyp-Gly at 1.4 a resolution: implications for collagen hydration
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Authors
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R.Berisio,
L.Vitagliano,
L.Mazzarella,
A.Zagari.
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Ref.
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biopolymers, 2001,
56,
8.
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