Milner-White, E.J., Pietras, Z., and Luisi, B.F. (2010) An ancient anion-binding structural module in RNA and DNA helicases. Proteins: Structure Function and Bioinformatics, 78(8), pp. 1900-1908. (doi:10.1002/prot.22704)
Full text not currently available from Enlighten.
RNA and DNA helicases manipulate or translocate along single strands of nucleic acids by grasping them using a conserved structural motif. We have examined the available crystal structures of helicases of the two principal superfamilies, SF1 and SF2, and observed that the most conserved interactions with the nucleic acid occur between the phosphosugar backbone of a trinucleotide and the three strand-helix loops within a (+¦-strand/+¦-helix)3 structural module. At the first and third loops is a conserved hydrogen-bonded feature called a thr-motif, often seen at +¦-helical N-termini, with the threonine as the N-cap residue. These loops can be aligned with few insertions or deletions, and their main chain atoms are structurally congruent amongst the family members and between the two modules found as tandem pairs in all SF1 and SF2 proteins. The other highly conserved interactions with nucleic acid involve mainchain NH groups, often at the helical N-termini, interacting with phosphate groups. We comment on how the sequence motifs that are commonly used to identify helicases map to locations on the module and discuss the implications of the conserved orientation of nucleic acid on the surface of the module for directional stepping along DNA or RNA.
|Glasgow Author(s) Enlighten ID:||Milner-White, Professor E|
|Authors:||Milner-White, E.J., Pietras, Z., and Luisi, B.F.|
|College/School:||College of Medical Veterinary and Life Sciences > School of Life Sciences|
|Journal Name:||Proteins: Structure Function and Bioinformatics|
|Published Online:||16 February 2010|