1us6
From Proteopedia
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| , resolution 1.65Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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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