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1rfy

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{{STRUCTURE_1rfy| PDB=1rfy | SCENE= }}
{{STRUCTURE_1rfy| PDB=1rfy | SCENE= }}
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'''Crystal Structure of Quorum-Sensing Antiactivator TraM'''
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===Crystal Structure of Quorum-Sensing Antiactivator TraM===
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==Overview==
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The quorum-sensing transcriptional activator TraR of Agrobacterium tumefaciens, which controls the replication and conjugal transfer of the tumour-inducing (Ti) virulence plasmid, is inhibited by the TraM antiactivator. The crystal structure of TraM reveals this protein to form a homodimer in which the monomer primarily consists of two long coiled alpha-helices, and one of the helices from each monomer also bundles to form the dimeric interface. The importance of dimerization is addressed by mutational studies in which disruption of the hydrophobic dimer interface leads to aggregation of TraM. Biochemical studies confirm that TraM exists as a homodimer in solution in equilibrium with the monomeric form, and also establish that the TraM-TraR complex is a heterodimer. Thus, the TraM homodimer undergoes dissociation in forming the antiactivation complex. Combined with the structure of TraR (Zhang et al., 2002, Nature 417: 971-974; Vannini et al., 2002, EMBO J 21: 4393-4401), our structural analysis suggests overlapping interactive surfaces in homodimeric TraM with those in the TraM-TraR complex and a mechanism for TraM inhibition on TraR.
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(as it appears on PubMed at http://www.pubmed.gov), where 15186414 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15186414}}
==About this Structure==
==About this Structure==
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[[Category: Homodimer]]
[[Category: Homodimer]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 19:07:44 2008''

Revision as of 16:07, 28 July 2008

Image:1rfy.png

Template:STRUCTURE 1rfy

Crystal Structure of Quorum-Sensing Antiactivator TraM

Template:ABSTRACT PUBMED 15186414

About this Structure

1RFY is a Single protein structure of sequence from Agrobacterium tumefaciens. Full crystallographic information is available from OCA.

Reference

Quorum-sensing antiactivator TraM forms a dimer that dissociates to inhibit TraR., Chen G, Malenkos JW, Cha MR, Fuqua C, Chen L, Mol Microbiol. 2004 Jun;52(6):1641-51. PMID:15186414

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