1us6
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(New page: 200px<br /><applet load="1us6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1us6, resolution 1.65Å" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 02:10, 21 November 2007
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CRYSTAL STRUCTURE OF THE QUORUM-SENSING PROTEIN TRAM FROM AGROBACTERIUM TUMEFACIENS AT 1.65 ANG. RESOLUTION
Overview
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.
About this Structure
1US6 is a Single protein structure of sequence from Agrobacterium tumefaciens. Full crystallographic information is available from OCA.
Reference
Crystal structure of the quorum-sensing protein TraM and its interaction with the transcriptional regulator TraR., Vannini A, Volpari C, Di Marco S, J Biol Chem. 2004 Jun 4;279(23):24291-6. Epub 2004 Mar 24. PMID:15044488
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