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Purification, crystallization and preliminary X‐ray diffraction of the N‐terminal calmodulin‐like domain of the human mitochondrial ATP‐Mg/P i carrier SCaMC1
Author(s) -
Yang Qin,
Brüschweiler Sven,
Chou James J.
Publication year - 2014
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x1303241x
Subject(s) - calmodulin , crystallization , transmembrane domain , crystallography , transmembrane protein , inner mitochondrial membrane , chemistry , x ray crystallography , helix (gastropod) , biophysics , mitochondrion , stereochemistry , biochemistry , biology , diffraction , membrane , physics , enzyme , receptor , organic chemistry , optics , ecology , snail
SCaMC is an ATP‐Mg/P i carrier protein located at the mitochondrial inner membrane. SCaMC has an unusual N‐terminal Ca 2+ ‐binding domain (NTD) in addition to its characteristic six‐helix transmembrane bundle. The NTD of human SCaMC1 (residues 1–193) was expressed and purified in order to study its role in Ca 2+ ‐regulated ATP‐Mg/P i transport mediated by its transmembrane domain. While Ca 2+ ‐bound NTD could be crystallized, the apo state resisted extensive crystallization trials. Selenomethionine‐labeled Ca 2+ ‐bound NTD crystals, which belonged to space group P 6 2 22 with one molecule per asymmetric unit, diffracted X‐rays to 2.9 Å resolution.