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'''Structure of the Vibrio cholerae virulence activator AphA''' | '''Structure of the Vibrio cholerae virulence activator AphA''' | ||
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[[Category: Skorupski, K.]] | [[Category: Skorupski, K.]] | ||
[[Category: Taylor, R T.]] | [[Category: Taylor, R T.]] | ||
[[Category: | [[Category: Transcription factor]] | ||
[[Category: | [[Category: Vibrio cholerae]] | ||
[[Category: | [[Category: Virulence factor]] | ||
[[Category: | [[Category: Winged helix]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:16:32 2008'' | |||
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Revision as of 16:16, 3 May 2008
Structure of the Vibrio cholerae virulence activator AphA
OverviewOverview
AphA is a member of a new and largely uncharacterized family of transcriptional activators that is required for initiating virulence gene expression in Vibrio cholerae, the causative agent of the frequently fatal epidemic diarrheal disease cholera. AphA activates transcription by an unusual mechanism that appears to involve a direct interaction with the LysR-type regulator AphB at the tcpPH promoter. As a first step toward understanding the molecular basis for tcpPH activation by AphA and AphB, we have determined the crystal structure of AphA to 2.2 angstrom resolution. AphA is a dimer with an N-terminal winged helix DNA binding domain that is architecturally similar to that of the MarR family of transcriptional regulators. Unlike this family, however, AphA has a unique C-terminal antiparallel coiled coil domain that serves as its primary dimerization interface. AphA monomers are highly unstable by themselves and form a linked topology, requiring the protein to partially unfold to form the dimer. The structure of AphA also provides insights into how it cooperates with AphB to activate transcription, most likely by forming a heterotetrameric complex at the tcpPH promoter.
About this StructureAbout this Structure
1YG2 is a Single protein structure of sequence from Vibrio cholerae. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the virulence gene activator AphA from Vibrio cholerae reveals it is a novel member of the winged helix transcription factor superfamily., De Silva RS, Kovacikova G, Lin W, Taylor RK, Skorupski K, Kull FJ, J Biol Chem. 2005 Apr 8;280(14):13779-83. Epub 2005 Jan 12. PMID:15647287 Page seeded by OCA on Sat May 3 16:16:32 2008