Open AccessPurification, crystallization and preliminary crystallographic analysis of the CBS‐domain pair of cyclin M2 (CNNM2)
Author(s) -
GómezGarcía Inmaculada,
Stuiver Marchel,
Ereño June,
Oyenarte Iker,
CorralRodríguez María Angeles,
Müller Dominik,
MartínezCruz Luis Alfonso
Publication year - 2012
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309112035348
Subject(s) - crystallography , gene , magnesium , crystallization , chemistry , crystal structure , biology , genetics , organic chemistry
This work describes the purification and preliminary crystallographic analysis of the CBS‐domain pair of the murine CNNM2 magnesium transporter (formerly known as ancient domain protein 2; ACDP2), which consists of a pair of cystathionine β‐synthase (CBS) motifs and has 100% sequence identity to its human homologue. CNNM proteins represent the least‐studied members of the eight different types of magnesium transporters identified to date in mammals. In humans, the CNNM family is encoded by four genes: CNNM1–4 . CNNM1 acts as a cytosolic copper chaperone, whereas CNNM2 and CNNM4 have been associated with magnesium handling. Interestingly, mutations in the CNNM2 gene cause familial dominant hypomagnesaemia (MIM:607803), a rare human disorder characterized by renal and intestinal magnesium (Mg 2+ ) wasting, which may lead to symptoms of Mg 2+ depletion such as tetany, seizures and cardiac arrhythmias. This manuscript describes the preliminary crystallographic analysis of two different crystal habits of a truncated form of the protein containing its regulatory CBS‐domain pair, which has been reported to host the pathological mutation T568I in humans. The crystals belonged to space groups P 2 1 2 1 2 and I 222 (or I 2 1 2 1 2 1 ) and diffracted X‐rays to 2.0 and 3.6 Å resolution, respectively, using synchrotron radiation.