Structure of the exon junction core complex with a trapped DEAD-Box ATPase bound to RNA

Science

Volumn 313, Issue 5795, 2006, Pages 1968-1972

  Andersen, Christian B F ^a   Ballut, Lionel ^a,b   Johansen, Jesper S ^a   Chamieh, Hala ^b   Nielsen, Klaus H ^a   Oliveira, Cristiano L P ^a   Pedersen, Jan Skov ^a   Séraphin, Bertrand ^b   Hir, Hervé Le ^b   Andersen, Gregers Rom ^a  

^a AARHUS UNIVERSITY   (Denmark)

^b CENTRE DE GÉNÉTIQUE MOLÉCULAIRE   (France)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINETRIPHOSPHATE; COMPLEXATION; GENETIC ENGINEERING; PROTEINS;

BINDING PLATFORM; EUKARYOTES; EXON JUNCTION; NUCLEOTIDES;

RNA;

ADENOSINE TRIPHOSPHATASE; DEAD BOX PROTEIN; DOUBLE STRANDED RNA; INITIATION FACTOR 4A; MESSENGER RNA; MULTIPROTEIN COMPLEX; RNA;

EUKARYOTE; GENETIC STRUCTURE; PROTEIN; RNA;

ARTICLE; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; DROSOPHILA; EXON; HYDROGEN BOND; HYDROLYSIS; PRIORITY JOURNAL; PROTEIN MOTIF; PROTEIN RNA BINDING; RNA SPLICING; RNA TRANSPORT; STEREOCHEMISTRY; X RAY CRYSTALLOGRAPHY;

ADENOSINE TRIPHOSPHATE; ADENYLYL IMIDODIPHOSPHATE; AMINO ACID MOTIFS; AMINO ACID SEQUENCE; ANIMALS; CRYSTALLOGRAPHY, X-RAY; DEAD-BOX RNA HELICASES; DIMERIZATION; DROSOPHILA PROTEINS; EUKARYOTIC INITIATION FACTOR-4A; EXONS; HUMANS; HYDROGEN BONDING; HYDROLYSIS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; NEOPLASM PROTEINS; NUCLEAR PROTEINS; NUCLEIC ACID CONFORMATION; POLY U; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; RNA HELICASES; RNA, MESSENGER; RNA-BINDING PROTEINS;

EUKARYOTA;

EID: 33749332762     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.1131981     Document Type: Article

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30. We thank G. Hartvigsen for technical assistance; W. Merrick and E. Jankowsky for discussion and suggestions; T. Boesen, F. Fredslund, and the staffs at CASSIOPEIA, European Synchrotron Radiation Facility, and
31. Swiss Light Source for help with data collection. G.R.A. and J.S.P. were supported by the Danish Natural Science Research Council and the Danish National Research Foundation. H.L.H. was supported by the CNRS, the French Research Ministry (grant ACI-Jeunes Chercheurs), the Agence Nationale de la Recherche, and the European Alternative Spiking Network. Structure factors and coordinates are deposited at the Protein Data Bank as entries 2HYI and 2HXY.