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2P6N

Human DEAD-box RNA helicase DDX41, helicase domain

Summary for 2P6N
Entry DOI10.2210/pdb2p6n/pdb
DescriptorATP-dependent RNA helicase DDX41 (1 entity in total)
Functional Keywordsrna, helicase, dead, structural genomics, structural genomics consortium, sgc, hydrolase
Biological sourceHomo sapiens (human)
Cellular locationNucleus (Potential): Q9UJV9
Total number of polymer chains2
Total formula weight42344.55
Authors
Primary citationSchutz, P.,Karlberg, T.,van den Berg, S.,Collins, R.,Lehtio, L.,Hogbom, M.,Holmberg-Schiavone, L.,Tempel, W.,Park, H.W.,Hammarstrom, M.,Moche, M.,Thorsell, A.G.,Schuler, H.
Comparative Structural Analysis of Human DEAD-Box RNA Helicases.
Plos One, 5:12791-12791, 2010
Cited by
PubMed Abstract: DEAD-box RNA helicases play various, often critical, roles in all processes where RNAs are involved. Members of this family of proteins are linked to human disease, including cancer and viral infections. DEAD-box proteins contain two conserved domains that both contribute to RNA and ATP binding. Despite recent advances the molecular details of how these enzymes convert chemical energy into RNA remodeling is unknown. We present crystal structures of the isolated DEAD-domains of human DDX2A/eIF4A1, DDX2B/eIF4A2, DDX5, DDX10/DBP4, DDX18/myc-regulated DEAD-box protein, DDX20, DDX47, DDX52/ROK1, and DDX53/CAGE, and of the helicase domains of DDX25 and DDX41. Together with prior knowledge this enables a family-wide comparative structural analysis. We propose a general mechanism for opening of the RNA binding site. This analysis also provides insights into the diversity of DExD/H- proteins, with implications for understanding the functions of individual family members.
PubMed: 20941364
DOI: 10.1371/journal.pone.0012791
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.6 Å)
Structure validation

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