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PDBsum entry 1v6q
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Structural protein
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PDB id
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1v6q
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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 structures of collagen model peptides with pro-Hyp-Gly repeating sequence at 1.26 a resolution: implications for proline ring puckering.
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Authors
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K.Okuyama,
C.Hongo,
R.Fukushima,
G.Wu,
H.Narita,
K.Noguchi,
Y.Tanaka,
N.Nishino.
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Ref.
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Biopolymers, 2004,
76,
367-377.
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PubMed id
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Abstract
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Triple-helical structures of (Pro-Hyp-Gly)n (n = 10, 11) at 100 K and room
temperature (RT) were analyzed at 1.26 A resolution by using synchrotron
radiation data. Totals of 49 and 42 water molecules per seven triplets in an
asymmetric unit were found for the structures at 100 K and RT, respectively.
These water molecules were classified into two groups, those in the first and
second hydration shells. Although there was no significant difference between
water molecules in the first shell at 100 K and those at RT, a significant
difference between those in the second shell was observed. That is, the number
of water molecules at RT decreased to one half and the average distance from
peptide chains at RT became longer by about 0.3 A. On the other hand, of seven
triplets in an asymmetric unit, three proline residues at the X position at 100
K clearly showed an up-puckering conformation, as opposed to the recent
propensity-based hypothesis for the stabilization and destabilization of
triple-helical structures by proline hydroxylation. This puckering was
attributed to the interaction between proline rings and the surrounding water
molecules at 100 K, which is much weaker at RT, as shown by longer average
distance from peptide chains.
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Headers
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