Rop protein

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Rop (also known as repressor of primer) is a small protein responsible for keeping the copy number of ColE1 and related bacterial plasmids low in E. coli. Structurally, Rop is a homodimeric four-helix bundle protein formed by the antiparallel interaction of two helix-turn-helix monomers. The Rop protein's structure has been solved to high resolution.[1] Due to its small size and known structure, Rop has been used in protein design work to rearrange its helical topology and reengineer its loop regions.[2] In general, the four-helix bundle has been extensively used in de novo protein design work as a simple model to understand the relationship between amino acid sequence and structure.

References[edit]

  1. ^ Banner, David W.; Kokkinidis, Michael; Tsernoglou, Demetrius (August 1987). "Structure of the ColE1 Rop protein at 1.7 Å resolution". Journal of Molecular Biology. 196 (3): 657–675. doi:10.1016/0022-2836(87)90039-8. PMID 3681971. 
  1. ^ Kresse, H. P.; Czubayko, M.; Nyakatura, G.; Vriend, G.; Sander, C.; Bloecker, H. (1 November 2001). "Four-helix bundle topology re-engineered: monomeric Rop protein variants with different loop arrangements". Protein Engineering Design and Selection. 14 (11): 897–901. doi:10.1093/protein/14.11.897. PMID 11742109.