2ns1

From Proteopedia

(Difference between revisions)

Revision as of 06:11, 10 February 2016

Crystal structure of the e. coli ammonia channel AMTB complexed with the signal transduction protein GLNK

Structural highlights

2ns1 is a 2 chain structure with sequence from Ecoli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Related:	1u7g, 1xqf, 1gnk, 2gnk, 2b2h
Gene:	amtB (ECOLI), glnK (ECOLI)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[AMTB_ECOLI] Involved in the uptake of ammonia. [GLNK_ECOLI] P-II indirectly controls the transcription of the glutamine synthetase gene (glnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of GlnA. When P-II is uridylylated to P-II-UMP, these events are reversed. When the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP, which causes the deadenylation of glutamine synthetase by GlnE, so activating the enzyme (By similarity).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Ammonia conductance is highly regulated. A P(II) signal transduction protein, GlnK, is the final regulator of transmembrane ammonia conductance by the ammonia channel AmtB in Escherichia coli. The complex formed between AmtB and inhibitory GlnK at 1.96-A resolution shows that the trimeric channel is blocked directly by GlnK and how, in response to intracellular nitrogen status, the ability of GlnK to block the channel is regulated by uridylylation/deuridylylation at Y51. ATP and Mg(2+) augment the interaction of GlnK. The hydrolyzed product, adenosine 5'-diphosphate orients the surface of GlnK for AmtB blockade. 2-Oxoglutarate diminishes AmtB/GlnK association, and sites for 2-oxoglutarate are evaluated.

Inhibitory complex of the transmembrane ammonia channel, AmtB, and the cytosolic regulatory protein, GlnK, at 1.96 A.,Gruswitz F, O'Connell J 3rd, Stroud RM Proc Natl Acad Sci U S A. 2007 Jan 2;104(1):42-7. Epub 2006 Dec 26. PMID:17190799^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Gruswitz F, O'Connell J 3rd, Stroud RM. Inhibitory complex of the transmembrane ammonia channel, AmtB, and the cytosolic regulatory protein, GlnK, at 1.96 A. Proc Natl Acad Sci U S A. 2007 Jan 2;104(1):42-7. Epub 2006 Dec 26. PMID:17190799

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2ns1"

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     <text>to colour the structure by Evolutionary Conservation</text>
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-</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2ns1 ConSurf].
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2ns1

From Proteopedia

Revision as of 06:11, 10 February 2016

Crystal structure of the e. coli ammonia channel AMTB complexed with the signal transduction protein GLNK

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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