Crystallization and preliminary X-ray analysis of the Ca2+-bound C-terminal lobe of troponin C in complex with a troponin I-derived peptide fragment from Akazara scallop.
Troponin C (TnC) is the Ca(2+)-binding component of troponin and triggers muscle contraction. TnC of the invertebrate Akazara scallop can bind only one Ca(2+) at the C-terminal EF-hand motif. Recombinant TnC was expressed in Escherichia coli, purified, complexed with a 24-residue synthetic peptide derived from scallop troponin I (TnI) and crystallized. The crystals diffracted X-rays to 1.80 A resolution and belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 32.1, b = 42.2, c = 60.0 A. The asymmetric unit was assumed to contain one molecular complex of the Akazara scallop TnC C-lobe and TnI fragment, with a Matthews coefficient of 1.83 A(3) Da(-1) and a solvent content of 33.0%.
Yumoto
Fumiaki
F
Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, Bunkyo-ku, Tokyo, Japan.
Nagata
Koji
K
Miyauchi
Yumiko
Y
Ojima
Takao
T
Tanaka
Hiroyuki
H
Nishita
Kiyoyoshi
K
Ohtsuki
Iwao
I
Tanokura
Masaru
M
D000818:Animals; D001665:Binding Sites; D002118:Calcium / Q000378:metabolism*; D003460:Crystallization; D046912:Multiprotein Complexes / Q000737:chemistry* / Q000378:metabolism; D049897:Pectinidae / Q000737:chemistry*; D010446:Peptide Fragments / Q000737:chemistry* / Q000378:metabolism; D019209:Troponin C / Q000737:chemistry* / Q000378:metabolism; D019210:Troponin I / Q000737:chemistry* / Q000378:metabolism
D046912:Multiprotein Complexes; D010446:Peptide Fragments; D019209:Troponin C; D019210:Troponin I; D002118:Calcium