ToxT: Difference between revisions

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<StructureSection load='3gbg' color='structure' size='500' frame='true' align='right' caption='ToxT, 1.9 Angstrom resolution crystal structure' >
<StructureSection load='3gbg' color='structure' size='500' frame='true' align='right' caption='ToxT, 1.9 Angstrom resolution crystal structure' >
==Structural Features==
==Structural Features==
<u>DNA-binding</u>. ToxT belongs to a family of transcriptional regulators headed by and known as AraC.<ref name="structure">PMID: 20133655</ref> The AraC family is characterized by a 100 amino acid region of sequence similarity that forms a <scene name='ToxT_Transcriptional_Regulator_in_Vibrio_cholerae/Two_hth_domains/1'>DNA-binding domain</scene> with two helix-turn-helix motifs (one on either side of the black linker). <ref name="arac">PMID: 11282467</ref> The two HTH regions are linked by a very polar alpha helix (shown in black). The overall domain is located at the C-terminus.<ref name="structure">PMID: 20133655</ref> Assuming ToxT is similar in mechanism to other AraC proteins, helix six from HTH1 and helix nine from HTH2 become aligned with the help of helix seven (the polar linking region) to allow binding to major consecutive grooves of target DNA.<ref name="structure">PMID: 20133655</ref>[http://www.pnas.org/content/107/7/2860/F3.large.jpg]. The conformation of helix seven is dependent on the ligand bound.
<u>DNA-binding</u>. ToxT belongs to a family of transcriptional regulators headed by and known as AraC.<ref name="structure">PMID: 20133655</ref> The AraC family is characterized by a 100 amino acid region of sequence similarity that forms a <scene name='ToxT_Transcriptional_Regulator_in_Vibrio_cholerae/Two_hth_domains/1'>DNA-binding domain</scene> with two helix-turn-helix motifs (one on either side of the black linker). <ref name="arac">PMID: 11282467</ref> The two HTH regions are linked by a very polar alpha helix (shown in black). The overall domain is located at the C-terminus.<ref name="structure">PMID: 20133655</ref> Assuming ToxT is similar in mechanism to other AraC proteins, helix six from HTH1 and helix nine from HTH2 become aligned with the help of helix seven (the polar linking region) to allow binding to major consecutive grooves of target DNA (specific promoters for virulence genes).<ref name="structure">PMID: 20133655</ref>[http://www.pnas.org/content/107/7/2860/F3.large.jpg]. The conformation of helix seven is dependent on the ligand bound.
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