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PDBsum entry 3a19
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Structural protein
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PDB id
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3a19
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Contents |
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25 a.a.
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24 a.a.
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26 a.a.
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26 a.a.
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25 a.a.
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References listed in PDB file
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Key reference
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Title
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Two crystal modifications of (pro-Pro-Gly)4-Hyp-Hyp-Gly-(Pro-Pro-Gly)4 reveal the puckering preference of hyp(X) in the hyp(X):hyp(y) and hyp(X):pro(y) stacking pairs in collagen helices.
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Authors
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K.Okuyama,
T.Morimoto,
H.Narita,
T.Kawaguchi,
K.Mizuno,
H.P.Bächinger,
G.Wu,
K.Noguchi.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 2010,
66,
88-96.
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PubMed id
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Abstract
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Two crystal modifications of a collagen model peptide,
(Pro-Pro-Gly)(4)-Hyp-Hyp-Gly-(Pro-Pro-Gly)(4) [where Hyp is
(4R,2S)-L-hydroxyproline], showed very similar unit-cell parameters and belonged
to the same space group P2(1). Both crystals exhibited pseudo-merohedral
twinning. The main difference was in their molecular-packing arrangements. One
modification showed pseudo-hexagonal packing, while the other showed
pseudo-tetragonal packing. Despite their different packing arrangements, no
significant differences were observed in the hydration states of these
modifications. The peptide in the pseudo-tetragonal crystal showed a cyclic
fluctuation of helical twists with a period of 20 A, while that in the
pseudo-hexagonal crystal did not. In these modifications, the puckering
conformations of four of the 12 Hyp residues at the X position of the
Hyp(X)-Hyp(Y)-Gly sequence were in the opposite conformations to the previous
hypothesis that Hyp(X) residues involved in Hyp(X):Hyp(Y) and Hyp(X):Pro(Y)
stacking pairs prefer up-puckering and down-puckering conformations,
respectively. Detailed investigation of the molecular interactions between
Hyp(X) and adjacent molecules revealed that these opposite conformations
appeared because the puckering conformation, which follows the hypothesis, is
subject to steric hindrance from the adjacent molecule.
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