1qo0

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==Overview==
==Overview==
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Inducible expression of the aliphatic amidase operon in Pseudomonas, aeruginosa is controlled by an antitermination mechanism which allows, production of the full-length transcript only in the presence of, small-molecule inducers, such as acetamide. Ligand-regulated, antitermination is provided by AmiC, the ligand-sensitive negative, regulator, and AmiR, the RNA-binding positive regulator. Under, non-inducing or repressing growth conditions, AmiC and AmiR form a complex, in which the activity of AmiR is silenced. The crystal structure of the, AmiC-AmiR complex identifies AmiR as a new and highly unusual member of, the response-regulator family of bacterial signal transduction proteins, regulated by sequestration rather than phosphorylation. Comparison with, the structure of free AmiC reveals the subtle mechanism of ligand-induced, release of AmiR.
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Inducible expression of the aliphatic amidase operon in Pseudomonas aeruginosa is controlled by an antitermination mechanism which allows production of the full-length transcript only in the presence of small-molecule inducers, such as acetamide. Ligand-regulated antitermination is provided by AmiC, the ligand-sensitive negative regulator, and AmiR, the RNA-binding positive regulator. Under non-inducing or repressing growth conditions, AmiC and AmiR form a complex in which the activity of AmiR is silenced. The crystal structure of the AmiC-AmiR complex identifies AmiR as a new and highly unusual member of the response-regulator family of bacterial signal transduction proteins, regulated by sequestration rather than phosphorylation. Comparison with the structure of free AmiC reveals the subtle mechanism of ligand-induced release of AmiR.
==About this Structure==
==About this Structure==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Pseudomonas aeruginosa]]
[[Category: Pseudomonas aeruginosa]]
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[[Category: Hara, B.P.O.]]
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[[Category: Hara, B P.O.]]
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[[Category: Pearl, L.H.]]
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[[Category: Pearl, L H.]]
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[[Category: Roe, S.M.]]
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[[Category: Roe, S M.]]
[[Category: BMD]]
[[Category: BMD]]
[[Category: binding protein]]
[[Category: binding protein]]
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[[Category: receptor]]
[[Category: receptor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:01:25 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:41:49 2008''

Revision as of 12:41, 21 February 2008


1qo0, resolution 2.25Å

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AMIDE RECEPTOR OF THE AMIDASE OPERON OF PSEUDOMONAS AERUGINOSA (AMIC) COMPLEXED WITH THE NEGATIVE REGULATOR AMIR.

Overview

Inducible expression of the aliphatic amidase operon in Pseudomonas aeruginosa is controlled by an antitermination mechanism which allows production of the full-length transcript only in the presence of small-molecule inducers, such as acetamide. Ligand-regulated antitermination is provided by AmiC, the ligand-sensitive negative regulator, and AmiR, the RNA-binding positive regulator. Under non-inducing or repressing growth conditions, AmiC and AmiR form a complex in which the activity of AmiR is silenced. The crystal structure of the AmiC-AmiR complex identifies AmiR as a new and highly unusual member of the response-regulator family of bacterial signal transduction proteins, regulated by sequestration rather than phosphorylation. Comparison with the structure of free AmiC reveals the subtle mechanism of ligand-induced release of AmiR.

About this Structure

1QO0 is a Protein complex structure of sequences from Pseudomonas aeruginosa with as ligand. Known structural/functional Sites: and . Full crystallographic information is available from OCA.

Reference

Crystal structure and induction mechanism of AmiC-AmiR: a ligand-regulated transcription antitermination complex., O'Hara BP, Norman RA, Wan PT, Roe SM, Barrett TE, Drew RE, Pearl LH, EMBO J. 1999 Oct 1;18(19):5175-86. PMID:10508151

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