Open AccessCrystallization and preliminary crystallographic analysis of the global nitrogen regulator AmtR from Corynebacterium glutamicum
Author(s) -
Hasselt Kristin,
Sevvana Madhumati,
Burkovski Andreas,
Muller Yves A.
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s174430910903663x
Subject(s) - corynebacterium glutamicum , tetr , regulator , trimer , effector , transcriptional regulation , transcription factor , crystallization , chemistry , transcription (linguistics) , molecule , biochemistry , biology , stereochemistry , crystallography , repressor , dimer , gene , organic chemistry , linguistics , philosophy
AmtR, a member of the TetR family of transcription regulators, is a global regulator of nitrogen control in Corynebacterium glutamicum . Unlike other TetR‐family members, which are regulated by small‐molecule effectors, AmtR is regulated by a protein called GlnK. It has been shown that a GlnK trimer has to become adenylylated prior to formation of a complex with AmtR. The physiological function of AmtR has been very well studied, but structural characterization of the mechanistic aspects of AmtR‐regulated transcription has yet to be accomplished. AmtR has successfully been crystallized in space group P 2 1 2 1 2, with six molecules in the asymmetric unit and unit‐cell parameters a = 153.34, b = 163.10, c = 51.93 Å. Preliminary phases were obtained using Se‐SAD.