Rop protein
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Rop protein (also known as repressor of primer protein) is a small dimeric protein consisting of two coiled-coil motifs that dimerize to form four-helix bundles. Each monomer is 63 amino acids long and consists of a helix-turn-helix motif with a C-terminal tail. The protein is expressed in E. coli as a mechanism for preserving the gene copy numbers of plasmids. The Rop protein's structure has been solved to high resolution. Due to its small size, Rop has been used in protein design work to rearrange its helical topology and reengineer its loop regions.
[edit] References
- ^ Banner DW, Kokkinidis M, Tsernoglou D. (1987). Structure of the ColE1 rop protein at 1.7 A resolution. J Mol Biol 196(3):657-75.
- ^ Kresse HP, Czubayko M, Nyakatura G, Vriend G, Sander C, Bloecker H. (2001). Four-helix bundle topology re-engineered: monomeric Rop protein variants with different loop arrangements. Protein Eng 14(11):897-901.
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