title: Similarities in the structure of the transcriptional repressor AmtR in two different space groups suggest a model for the interaction with GlnK.
abstract: AmtR belongs to the TetR family of transcription regulators and is a global nitrogen regulator that is induced under nitrogen-starvation conditions in Corynebacterium glutamicum. AmtR regulates the expression of transporters and enzymes for the assimilation of ammonium and alternative nitrogen sources, for example urea, amino acids etc. The recognition of operator DNA by homodimeric AmtR is not regulated by small-molecule effectors as in other TetR-family members but by a trimeric adenylylated PII-type signal transduction protein named GlnK. The crystal structure of ligand-free AmtR (AmtRorth) has been solved at a resolution of 2.1 Å in space group P21212. Comparison of its quaternary assembly with the previously solved native AmtR structure (PDB entry 5dy1) in a trigonal crystal system (AmtRtri) not only shows how a solvent-content reduction triggers a space-group switch but also suggests a model for how dimeric AmtR might stoichiometrically interact with trimeric adenylylated GlnK.
authors.affiliation: Lehrstuhl für Biotechnik, Department of Biology, Friedrich-Alexander University Erlangen-Nuremberg, 91052 Erlangen, Germany.
authors.forename: Madhumati
authors.initials: M
authors.lastname: Sevvana
authors.affiliation: Professur für Mikrobiologie, Department of Biology, Friedrich-Alexander University Erlangen-Nuremberg, 91052 Erlangen, Germany.
authors.forename: Kristin
authors.initials: K
authors.lastname: Hasselt
authors.affiliation: Lehrstuhl für Biotechnik, Department of Biology, Friedrich-Alexander University Erlangen-Nuremberg, 91052 Erlangen, Germany.
authors.forename: Florian C
authors.initials: FC
authors.lastname: Grau
authors.affiliation: Professur für Mikrobiologie, Department of Biology, Friedrich-Alexander University Erlangen-Nuremberg, 91052 Erlangen, Germany.
authors.forename: Andreas
authors.initials: A
authors.lastname: Burkovski
authors.affiliation: Lehrstuhl für Biotechnik, Department of Biology, Friedrich-Alexander University Erlangen-Nuremberg, 91052 Erlangen, Germany.
authors.forename: Yves A
authors.initials: YA
authors.lastname: Muller
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D001665:Binding Sites; D003001:Cloning, Molecular; D048230:Corynebacterium glutamicum / Q000737:chemistry* / Q000378:metabolism; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D015870:Gene Expression; D008958:Models, Molecular; D051922:PII Nitrogen Regulatory Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D010957:Plasmids / Q000737:chemistry / Q000378:metabolism; D011485:Protein Binding; D000072756:Protein Conformation, alpha-Helical; D000072757:Protein Conformation, beta-Strand; D054730:Protein Interaction Domains and Motifs; D055503:Protein Multimerization; D020836:Protein Structure, Quaternary; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D012097:Repressor Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
chemical_list: C414398:AmtR protein, Corynebacterium glutamicum; D001426:Bacterial Proteins; D051922:PII Nitrogen Regulatory Proteins; D011994:Recombinant Proteins; D012097:Repressor Proteins
keywords: AmtR adenylylated GlnK complex stoichiometry; Corynebacterium glutamicum; crystal-packing comparison; nitrogen regulation; transcription regulator effector complex