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 1.65&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1us6.gif|left|200px]]<br /><applet load="1us6" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1us6, resolution 1.65&Aring;" />
caption="1us6, resolution 1.65&Aring;" />
'''CRYSTAL STRUCTURE OF THE QUORUM-SENSING PROTEIN TRAM FROM AGROBACTERIUM TUMEFACIENS AT 1.65 ANG. RESOLUTION'''<br />
'''CRYSTAL STRUCTURE OF THE QUORUM-SENSING PROTEIN TRAM FROM AGROBACTERIUM TUMEFACIENS AT 1.65 ANG. RESOLUTION'''<br />
==Overview==
==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.
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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.
==About this Structure==
==About this Structure==
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1US6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Agrobacterium_tumefaciens Agrobacterium tumefaciens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1US6 OCA].
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1US6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Agrobacterium_tumefaciens Agrobacterium tumefaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1US6 OCA].
==Reference==
==Reference==
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[[Category: Agrobacterium tumefaciens]]
[[Category: Agrobacterium tumefaciens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Marco, S.Di.]]
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[[Category: Marco, S Di.]]
[[Category: Vannini, A.]]
[[Category: Vannini, A.]]
[[Category: conjugation]]
[[Category: conjugation]]
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[[Category: transcripti regulation]]
[[Category: transcripti regulation]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 04:18:10 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:27:42 2008''

Revision as of 13:27, 21 February 2008


1us6, resolution 1.65Å

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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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