2RS6

Solution structure of the N-terminal dsRBD from RNA helicase A

Summary for 2RS6

• Entry DOI: 10.2210/pdb2rs6/pdb
• Related: 1whq 2RS7
• NMR Information: BMRB: 11456
• Descriptor: ATP-dependent RNA helicase A (1 entity in total)
• Functional Keywords: protein, double-stranded rna binding domain, dsrbd, dsrm, structural genomics, nppsfa, national project on protein structural and functional analyses, riken structural genomics/proteomics initiative, rsgi, hydrolase
• Biological source: Mus musculus (mouse)
• Cellular location: Nucleus, nucleolus: O70133
• Total number of polymer chains: 1
• Total formula weight: 10733.12

Authors

Nagata, T.,Muto, Y.,Tsuda, K.,Inoue, M.,Kigawa, T.,Terada, T.,Shirouzu, M.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2011-11-29, release date: 2012-03-14, Last modification date: 2024-05-15)

Primary citation

Nagata, T.,Tsuda, K.,Kobayashi, N.,Shirouzu, M.,Kigawa, T.,Guntert, P.,Yokoyama, S.,Muto, Y.
Solution structures of the double-stranded RNA-binding domains from RNA helicase A
Proteins, 80:1699-1706, 2012

PubMed Abstract: RNA helicase A (RHA) is a highly conserved protein with multifaceted functions in the gene expression of cellular and viral mRNAs. RHA recognizes highly structured nucleotides and catalytically rearranges the various interactions between RNA, DNA, and protein molecules to provide a platform for the ribonucleoprotein complex. We present the first solution structures of the double-stranded RNA-binding domains (dsRBDs), dsRBD1 and dsRBD2, from mouse RHA. We discuss the binding mode of the dsRBDs of RHA, in comparison with the known dsRBD structures in their complexes. Our structural data provide important information for the elucidation of the molecular reassembly mediated by RHA.

PubMed: 22454253
DOI: 10.1002/prot.24059

Experimental method

SOLUTION NMR