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| {{STRUCTURE_1us6| PDB=1us6 | SCENE= }} | | {{STRUCTURE_1us6| PDB=1us6 | SCENE= }} |
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| '''CRYSTAL STRUCTURE OF THE QUORUM-SENSING PROTEIN TRAM FROM AGROBACTERIUM TUMEFACIENS AT 1.65 ANG. RESOLUTION'''
| | ===CRYSTAL STRUCTURE OF THE QUORUM-SENSING PROTEIN TRAM FROM AGROBACTERIUM TUMEFACIENS AT 1.65 ANG. RESOLUTION=== |
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| ==Overview==
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| Transfer of the tumor-inducing plasmid in Agrobacterium tumefaciens is controlled by a quorum-sensing system whose main components are the transcriptional regulator TraR and its autoinducer. This system allows bacteria to synchronize infection of the host plant when a "quorum" of cells has been reached. TraM is an A. tumefaciens protein involved in the regulation of this system because it binds to TraR and prevents it from binding DNA. As a first step to understanding the molecular basis for the regulation of TraR by TraM, we have determined the crystal structure of TraM at 1.65 A resolution. This protein is packed as a dimer, with each monomer consisting mainly of two antiparallel alpha helices. Monomers are tightly associated, with a large hydrophobic area buried upon dimerization. Secondly, we characterized the TraR-TraM complex in vitro. TraM (11.4 kDa, monomer molecular mass) binds tightly TraR (27 kDa, monomer molecular mass) forming a stable oligomeric complex that likely accounts for two TraR and two TraM dimers.
| | The line below this paragraph, {{ABSTRACT_PUBMED_15044488}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 15044488 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_15044488}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Repressor]] | | [[Category: Repressor]] |
| [[Category: Transcripti regulation]] | | [[Category: Transcripti regulation]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:36:59 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 23:58:29 2008'' |
