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2nuu

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[[Image:2nuu.gif|left|200px]]<br /><applet load="2nuu" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2nuu.gif|left|200px]]
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caption="2nuu, resolution 2.50&Aring;" />
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'''Regulating the Escherichia coli ammonia channel: the crystal structure of the AmtB-GlnK complex'''<br />
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{{Structure
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|PDB= 2nuu |SIZE=350|CAPTION= <scene name='initialview01'>2nuu</scene>, resolution 2.50&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene>
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|ACTIVITY=
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|GENE= amtB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]), glnK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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}}
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'''Regulating the Escherichia coli ammonia channel: the crystal structure of the AmtB-GlnK complex'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2NUU is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=ADP:'>ADP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NUU OCA].
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2NUU is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NUU OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17220269 17220269]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/17220269 17220269]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: nitrogen regulation]]
[[Category: nitrogen regulation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:11:20 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:51:26 2008''

Revision as of 15:51, 20 March 2008


PDB ID 2nuu

Drag the structure with the mouse to rotate
, resolution 2.50Å
Ligands:
Gene: amtB (Escherichia coli), glnK (Escherichia coli)
Coordinates: save as pdb, mmCIF, xml



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

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