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'''Regulating the Escherichia coli ammonia channel: the crystal structure of the AmtB-GlnK complex''' | '''Regulating the Escherichia coli ammonia channel: the crystal structure of the AmtB-GlnK complex''' | ||
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[[Category: Merrick, M.]] | [[Category: Merrick, M.]] | ||
[[Category: Winkler, F K.]] | [[Category: Winkler, F K.]] | ||
[[Category: | [[Category: Ammonia transport]] | ||
[[Category: | [[Category: Membrane protein complex]] | ||
[[Category: | [[Category: Nitrogen regulation]] | ||
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Revision as of 06:56, 4 May 2008
Regulating the Escherichia coli ammonia channel: the crystal structure of the AmtB-GlnK complex
Overview
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 PII 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 A. This structure of PII 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.
About this Structure
2NUU is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.
Reference
The crystal structure of the Escherichia coli AmtB-GlnK complex reveals how GlnK regulates the ammonia channel., Conroy MJ, Durand A, Lupo D, Li XD, Bullough PA, Winkler FK, Merrick M, Proc Natl Acad Sci U S A. 2007 Jan 23;104(4):1213-8. Epub 2007 Jan 12. PMID:17220269 Page seeded by OCA on Sun May 4 09:56:11 2008
