Open AccessPurification, crystallization and preliminary crystallographic analysis of protein MJ1225 from Methanocaldococcus jannaschii , a putative archaeal homologue of γ‐AMPK
Author(s) -
Gómez García Inmaculada,
Kortázar Danel,
Oyenarte Iker,
Mato José María,
MartínezChantar María Luz,
MartínezCruz Luis Alfonso
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109026475
Subject(s) - heterotrimeric g protein , protein subunit , protein kinase a , ampk , crystallography , serine , biochemistry , biology , threonine , chemistry , kinase , enzyme , signal transduction , g protein , gene
In mammals, AMP‐activated protein kinase (AMPK) is a heterotrimeric protein composed of a catalytic serine/threonine kinase subunit (α) and two regulatory subunits (β and γ). The γ subunit senses the intracellular energy status by competitively binding AMP and ATP and is thought to be responsible for allosteric regulation of the whole complex. This work describes the purification and preliminary crystallographic analysis of protein MJ1225 from Methanocaldococcus jannaschii , an archaeal homologue of γ‐AMPK. The purified protein was crystallized using the hanging‐drop vapour‐diffusion method. Diffraction data for MJ1225 were collected to 2.3 Å resolution using synchrotron radiation. The crystals belonged to space group H 32, with unit‐cell parameters a = b = 108.95, c = 148.08 Å, α = β = 90.00, γ = 120.00°. Preliminary analysis of the X‐ray data indicated that there was one molecule per asymmetric unit.