3IUY

Crystal structure of DDX53 DEAD-box domain

Summary for 3IUY

• Entry DOI: 10.2210/pdb3iuy/pdb
• Descriptor: Probable ATP-dependent RNA helicase DDX53, ADENOSINE MONOPHOSPHATE, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: rec-a-like, dead-box, structural genomics, structural genomics consortium, sgc, atp-binding, helicase, hydrolase, nucleotide-binding, nucleus, rna-binding
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus : Q86TM3
• Total number of polymer chains: 2
• Total formula weight: 52265.35

Authors

Schutz, P.,Karlberg, T.,Collins, R.,Arrowsmith, C.H.,Berglund, H.,Bountra, C.,Edwards, A.M.,Flodin, S.,Flores, A.,Graslund, S.,Hammarstrom, M.,Johansson, A.,Johansson, I.,Kallas, A.,Kraulis, P.,Kotenyova, T.,Kotzsch, A.,Markova, N.,Moche, M.,Nielsen, T.K.,Nordlund, P.,Nyman, T.,Persson, C.,Roos, A.K.,Siponen, M.I.,Svensson, L.,Thorsell, A.G.,Tresaugues, L.,Van Den Berg, S.,Wahlberg, E.,Weigelt, J.,Welin, M.,Wisniewska, M.,Schuler, H.M.,Structural Genomics Consortium (SGC) (deposition date: 2009-08-31, release date: 2009-10-20, Last modification date: 2024-02-21)

Primary citation

Schutz, 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

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

Experimental method

X-RAY DIFFRACTION (2.4 Å)