3FE2

Human DEAD-BOX RNA helicase DDX5 (P68), conserved domain I in complex with ADP

3FE2 の概要

• エントリーDOI: 10.2210/pdb3fe2/pdb
• 分子名称: Probable ATP-dependent RNA helicase DDX5, SULFATE ION, ADENOSINE-5'-DIPHOSPHATE, ... (5 entities in total)
• 機能のキーワード: rna helicase, dead, adp, atp-binding, hydrolase, nucleotide-binding, rna-binding, helicase, methylation, mrna processing, mrna splicing, nucleus, phosphoprotein, spliceosome, structural genomics, structural genomics consortium, sgc
• 由来する生物種: Homo sapiens (Human)
• 細胞内の位置: Nucleus, nucleolus: P17844
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 55720.88

構造登録者

Karlberg, T.,Siponen, M.I.,Arrowsmith, C.H.,Berglund, H.,Bountra, C.,Collins, R.,Dahlgren, L.G.,Edwards, A.M.,Flodin, S.,Flores, A.,Graslund, S.,Hammarstrom, M.,Johansson, A.,Johansson, I.,Kotenyova, T.,Lehtio, L.,Moche, M.,Nilsson, M.E.,Nordlund, P.,Nyman, T.,Persson, C.,Sagemark, J.,Thorsell, A.G.,Tresaugues, L.,Van Den Berg, S.,Weigelt, J.,Welin, M.,Wikstrom, M.,Wisniewska, M.,Schuler, H.,Structural Genomics Consortium (SGC) (登録日: 2008-11-27, 公開日: 2008-12-16, 最終更新日: 2023-11-01)

主引用文献

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:e12791-e12791, 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

実験手法

X-RAY DIFFRACTION (2.6 Å)