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Title
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Crystallization and preliminary X-ray diffraction data of the complex between human centrin 2 and a peptide from the protein XPC.
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Authors
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J.B.Charbonnier,
P.Christova,
A.Shosheva,
E.Stura,
M.H.Le Du,
Y.Blouquit,
P.Duchambon,
S.Miron,
C.T.Craescu.
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Ref.
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Acta Crystallogr Sect F Struct Biol Cryst Commun, 2006,
62,
649-651.
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PubMed id
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Abstract
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Centrins are highly conserved calcium-binding proteins involved in the
nucleotide-excision repair pathway as a subunit of the heterotrimer including
the XPC and hHR23B proteins. A complex formed by a Ca2+-bound human centrin 2
construct (the wild type lacking the first 25 amino acids) with a 17-mer peptide
derived from the XPC sequence (residues Asn847-Arg863) was crystallized. Data
were collected to 1.65 angstroms resolution from crystals grown in 30%
monomethyl polyethylene glycol (MPEG) 500, 100 mM NaCl and 100 mM Bicine pH 9.0.
Crystals are monoclinic and belong to space group C2, with two molecules in the
asymmetric unit. The unit-cell parameters are a = 60.28, b = 59.42, c = 105.14
angstroms, alpha = gamma = 90, beta = 94.67 degrees. A heavy-atom derivative was
obtained by co-crystallization with Sr2+. The substitution was rationalized by
calorimetry experiments, which indicate a binding constant for Sr2+ of 4.0 x
10(4) M(-1).
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