Download MendeleyA novel dimerization motif in the C-terminal domain of the Thermus thermophilus DEAD box helicase Hera confers substantial flexibility.
Klostermeier, D., Rudolph, M.G.(2009) Nucleic Acids Res 37: 421-430
- PubMed: 19050012
- DOI: https://doi.org/10.1093/nar/gkn947
- Primary Citation of Related Structures:
3EAQ, 3EAR, 3EAS - PubMed Abstract:
DEAD box helicases are involved in nearly all aspects of RNA metabolism. They share a common helicase core, and may comprise additional domains that contribute to RNA binding. The Thermus thermophilus helicase Hera is the first dimeric DEAD box helicase. Crystal structures of Hera fragments reveal a bipartite C-terminal domain with a novel dimerization motif and an RNA-binding module. We provide a first glimpse on the additional RNA-binding module outside the Hera helicase core. The dimerization and RNA-binding domains are connected to the C-terminal RecA domain by a hinge region that confers exceptional flexibility onto the helicase, allowing for different juxtapositions of the RecA-domains in the dimer. Combination of the previously determined N-terminal Hera structure with the C-terminal Hera structures allows generation of a model for the entire Hera dimer, where two helicase cores can work in conjunction on large RNA substrates.
Organizational Affiliation:
Division of Biophysical Chemistry, Biozentrum, University of Basel, CH-4056 Basel, Switzerland. dagmar.klostermeier@unibas.ch
