NDLI: Crystallization and preliminary X-ray crystallographic analysis of $Ca^{2+}-free$ primary $Ca^{2+}-sensor$ of $Na^{+}/Ca^{2+}$ exchanger

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Mima, Masashi Kawai, Chika Paku, Kumsun Tomoo, Koji Ishida, Toshimasa Sugiyama, Shigeru Matsumura, Hiroyoshi Kitatani, Tomoya Yoshikawa, Hiroshi Y. Maki, Syou Adachi, Hiroaki Takano, Kazufumi Murakami, Satoshi Inoue, Tsuyoshi Mori, Yusuke Kita, Satomi Iwamoto, Takahiro
Description	Country affiliation: Japan Author Affiliation: Mima M ( Department of Physical Chemistry, Osaka University of Pharmaceutical Sciences, Takatsuki, Osaka 569-1094, Japan.)
Abstract	The plasma-membrane Na(+)/Ca(2+) exchanger (NCX) regulates intracellular Ca(2+) levels in cardiac myocytes. Two Ca(2+)-binding domains (CBD1 and CBD2) exist in the large cytosolic loop of NCX. The binding of Ca(2+) to CBD1 results in conformational changes that stimulate exchange to exclude Ca(2+) ions, whereas CBD2 maintains the structure, suggesting that CBD1 is the primary Ca(2+)-sensor. In order to clarify the structural scaffold for the Ca(2+)-induced conformational transition of CBD1 at the atomic level, X-ray structural analysis of its Ca(2+)-free form was attempted; the structure of the Ca(2+)-bound form is already available. Recombinant CBD1 (NCX1 372-508) with a molecular weight of 16 kDa was crystallized by the sitting-drop vapour-diffusion method at 293 K. The crystals belonged to the hexagonal space group P6(2)22 or P6(4)22, with unit-cell parameters a = b = 56.99, c = 153.86 A, beta = 120 degrees , and contained one molecule per asymmetric unit (V(M) = 2.25 A(3) Da(-1)) with a solvent content of about 55% (V(S) = 45.57%). Diffraction data were collected within the resolution range 27.72-3.00 A using an R-AXIS detector and gave a data set with an overall R(merge) of 10.8% and a completeness of 92.8%.
File Format	HTM / HTML
ISSN	2053230X
e-ISSN	17443091
DOI	10.1107/S1744309108032934
Journal	Acta Crystallographica Section F Structural Biology and Crystallization Communications
Issue Number	Pt 12
Volume Number	64
Language	English
Publisher	Wiley
Publisher Date	2008-12-01
Publisher Place	Great Britain (UK)
Access Restriction	Open
Subject Keyword	Discipline Crystallography Discipline Biophysics Discipline Molecular Biology Discipline Biochemistry Calcium Metabolism Sodium-calcium Exchanger Chemistry Binding Sites Crystallization Escherichia Coli Protein Conformation Protein Structure, Tertiary Recombinant Proteins Isolation & Purification
Content Type	Text
Resource Type	Article
Subject	Genetics Structural Biology Medicine Biochemistry Biophysics Condensed Matter Physics

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