User:David McDonald/Replication Termination Protein: Difference between revisions
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<scene name='User:David_McDonald/Replication_Termination_Protein/Rainbow_monomer/7'>RTP</scene> contains 122 amino acid residues and is an example of a winged helix structure, in the α+β protein folding family, containing four <scene name='User:David_McDonald/Replication_Termination_Protein/Alpha_helices/5'>α-helices</scene> and two <scene name='User:David_McDonald/Replication_Termination_Protein/Beta_sheets/2'>β-strands</scene><sup>[1]</sup>. | <scene name='User:David_McDonald/Replication_Termination_Protein/Rainbow_monomer/7'>RTP</scene> contains 122 amino acid residues and is an example of a winged helix structure, in the α+β protein folding family, containing four <scene name='User:David_McDonald/Replication_Termination_Protein/Alpha_helices/5'>α-helices</scene> and two <scene name='User:David_McDonald/Replication_Termination_Protein/Beta_sheets/2'>β-strands</scene><sup>[1]</sup>. | ||
In a cell, RTP exists as a homodimer, where the monomer subunits are tightly associated through antiparallel coiled-coil interactions between the <scene name='User:David_McDonald/Replication_Termination_Protein/Dimerisation_domain/4'>C-terminal</scene> α-helices to form the functional <scene name='User:David_McDonald/Replication_Termination_Protein/Dimer_no_dna/1'>Dimer</scene>. This dimer is held together by <scene name='User:David_McDonald/Replication_Termination_Protein/Dimer_hydrophobic/1'>hydrophobic interactions</scene>. | In a cell, RTP exists as a homodimer, where the monomer subunits are tightly associated through antiparallel coiled-coil interactions between the <scene name='User:David_McDonald/Replication_Termination_Protein/Dimerisation_domain/4'>C-terminal</scene> α-helices to form the functional <scene name='User:David_McDonald/Replication_Termination_Protein/Dimer_no_dna/1'>Dimer</scene>. This dimer is held together by <scene name='User:David_McDonald/Replication_Termination_Protein/Dimer_hydrophobic/1'>hydrophobic interactions</scene>. | ||
For crystallographic studies, a mutant of RTP (C110S) was created to avoid possible unwanted disulfide bond formation. In this mutant, the Cysteine at position <scene name='User:David_McDonald/Replication_Termination_Protein/Dimer_c110s/1'>110</scene> was changed to a Serine residue. It was shown that this did not result in a change in solution dimerisation or DNA binding functionality<sup>[2]</sup>. | |||
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== Works Cited == | == Works Cited == | ||
1. Crystal structure of replication terminator protein of B. subtilis at 2.6 Å. | 1. Bussiere, DE, Bastia, D and White, SW. (1995)Crystal structure of replication terminator protein of B. subtilis at 2.6 Å. Cell. 80: 651-660. | ||
2. J.P. Vivian, A.F. Hastings, I.G. Duggin, R.G. Wake, M.C.J. Wilce, and J.A. Wilce (2003) “The impact of single cysteine residue mutations on the replication terminator protein” Biochem. Biophys. Res. Commun. 310(4):1096-1103 | |||
