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The crystal structure of the Escherichia coli AmtB-GlnK complex reveals how GlnK regulates the ammonia channel
- Source :
- Proceedings of the National Academy of Sciences of the United States of America. 104(4)
- Publication Year :
- 2007
-
Abstract
- Amt proteins are ubiquitous channels for the conduction of ammonia in archaea, eubacteria, fungi, and plants. In Escherichia coli , previous studies have indicated that binding of the P II signal transduction protein GlnK to the ammonia channel AmtB regulates the channel thereby controlling ammonium influx in response to the intracellular nitrogen status. Here, we describe the crystal structure of the complex between AmtB and GlnK at a resolution of 2.5 Å. This structure of P II in a complex with one of its targets reveals physiologically relevant conformations of both AmtB and GlnK. GlnK interacts with AmtB almost exclusively via a long surface loop containing Y51 (T-loop), the tip of which inserts deeply into the cytoplasmic pore exit, blocking ammonia conduction. Y51 of GlnK is also buried in the pore exit, explaining why uridylylation of this residue prevents complex formation.
- Subjects :
- Protein Conformation
PII Nitrogen Regulatory Proteins
Molecular Sequence Data
medicine.disease_cause
Crystallography, X-Ray
Protein structure
medicine
Escherichia coli
Amino Acid Sequence
Binding site
Peptide sequence
Cation Transport Proteins
Multidisciplinary
Binding Sites
biology
Escherichia coli Proteins
Biological Sciences
biology.organism_classification
Nucleotidyltransferases
Recombinant Proteins
Transport protein
Biochemistry
Cytoplasm
Biophysics
Pii nitrogen regulatory proteins
Protons
Archaea
Subjects
Details
- ISSN :
- 00278424
- Volume :
- 104
- Issue :
- 4
- Database :
- OpenAIRE
- Journal :
- Proceedings of the National Academy of Sciences of the United States of America
- Accession number :
- edsair.doi.dedup.....42d61ab1f0b0ada90ac3576f99044fe1