Summary for 2RB4
| Entry DOI | 10.2210/pdb2rb4/pdb |
| Descriptor | ATP-dependent RNA helicase DDX25, CHLORIDE ION, SULFATE ION, ... (5 entities in total) |
| Functional Keywords | rna helicase, rossmann fold, structural genomics, structural genomics consortium, sgc, alternative initiation, atp-binding, developmental protein, differentiation, hydrolase, mrna transport, nucleotide-binding, nucleus, phosphorylation, rna-binding, spermatogenesis, translation regulation, transport |
| Biological source | Homo sapiens (human) |
| Cellular location | Cytoplasm : Q9UHL0 |
| Total number of polymer chains | 2 |
| Total formula weight | 40660.72 |
| Authors | Lehtio, L.,Hogbom, M.,Uppenberg, J.,Arrowsmith, C.H.,Berglund, H.,Edwards, A.M.,Ehn, M.,Flodin, S.,Flores, A.,Graslund, S.,Hallberg, B.M.,Hammarstrom, M.,Kotenyova, T.,Nilsson-Ehle, P.,Nordlund, P.,Nyman, T.,Ogg, D.,Persson, C.,Sagemark, J.,Stenmark, P.,Sundstrom, M.,Thorsell, A.G.,Van den Berg, S.,Weigelt, J.,Holmberg-Schiavone, L.,Structural Genomics Consortium (SGC) (deposition date: 2007-09-18, release date: 2007-10-02, Last modification date: 2023-08-30) |
| 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 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: 20941364DOI: 10.1371/journal.pone.0012791 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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