3EAS

Novel dimerization motif in the DEAD box RNA helicase Hera: form 1, complete dimer, asymmetric

Summary for 3EAS

• Entry DOI: 10.2210/pdb3eas/pdb
• Related: 3eaq 3ear
• Descriptor: Hera (1 entity in total)
• Functional Keywords: dead box rna helicase, dimer, atp-binding, helicase, hydrolase, nucleotide-binding
• Biological source: Thermus thermophilus
• Total number of polymer chains: 2
• Total formula weight: 47734.55

Authors

Klostermeier, D.,Rudolph, M.G. (deposition date: 2008-08-26, release date: 2008-12-09, Last modification date: 2023-08-30)

Primary citation

Klostermeier, D.,Rudolph, M.G.
A novel dimerization motif in the C-terminal domain of the Thermus thermophilus DEAD box helicase Hera confers substantial flexibility.
Nucleic Acids Res., 37:421-430, 2009

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.

PubMed: 19050012
DOI: 10.1093/nar/gkn947

Experimental method

X-RAY DIFFRACTION (2.8 Å)