Crystallization and preliminary crystallographic analysis of the global nitrogen regulator AmtR from Corynebacterium glutamicum.
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 P2(1)2(1)2, with six molecules in the asymmetric unit and unit-cell parameters a = 153.34, b = 163.10, c = 51.93 angstrom . Preliminary phases were obtained using Se-SAD.
Hasselt
Kristin
K
Lehrstuhl für Mikrobiologie, Friedrich-Alexander-Universität Erlangen-Nürnberg, Germany.
Sevvana
Madhumati
M
Burkovski
Andreas
A
Muller
Yves A
YA
D001426:Bacterial Proteins / Q000737:chemistry*; D048230:Corynebacterium glutamicum / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D015964:Gene Expression Regulation, Bacterial; D008969:Molecular Sequence Data; D009584:Nitrogen / Q000378:metabolism; D009713:Nucleotidyltransferases / Q000737:chemistry; D051922:PII Nitrogen Regulatory Proteins / Q000737:chemistry; D011487:Protein Conformation; D012097:Repressor Proteins / Q000737:chemistry*; D014961:X-Ray Diffraction
C414398:AmtR protein, Corynebacterium glutamicum; D001426:Bacterial Proteins; D051922:PII Nitrogen Regulatory Proteins; D012097:Repressor Proteins; D009713:Nucleotidyltransferases; D009584:Nitrogen