PDB-2ix8: MODEL FOR EEF3 BOUND TO AN 80S RIBOSOME

Entry
Summary
Database / ID	PORTEIN DATA BANK (PDB) / 2ix8
Title	MODEL FOR EEF3 BOUND TO AN 80S RIBOSOME
Descriptor	ELONGATION FACTOR 3A
Keywords	NUCLEOTIDE-BINDING, PROTEIN BIOSYNTHESIS, PHOSPHORYLATION, ELONGATION FACTOR, RNA-BINDING, ATP-BINDING, RRNA-BINDING
Authors	Andersen, C.B.F., Becker, T., Blau, M., Anand, M., Halic, M., Balar, B., Mielke, T., Boesen, T., Pedersen, J.S., Spahn, C.M.T., Kinzy, T.G., Andersen, G.R., Beckmann, R.
Date	Deposition: 2006-07-07, Release: 2007-07-10
PDBj Mine pages	Summary, Structural Details, Experimental Details, Functional Details
Other databases	RCSB-PDB, PDBe, CATH, CE, FSSP, SCOP, VAST
Sequence details	PDB LACKS THE C-TERMINAL PART OF EEF3 (RESIDUES 977-1044)
Structure Visualization
Movies	Movie Page #1: Depositted structure unit, Made by Jmol #2: Superimposing with simplified surface model of EM map, EMDB-1233, Made by Jmol #3: Superimposing with EM 3D map: EMDB-1233, Made by UCSF CHIMERA
Structure viewers	Yorodumi, jV4, Jmol, Biological unit (Images, jV)
Related Structure Data
Related Entries	EMDB-1233 CiteFit PDB-2iw3 Cite PDB-2iwh Cite PDB-2ix3 Cite Cite: data citing same article Fit: target map of fitting
Similar strucutres (beta)	Diagram PDB-2p8y PDB-2p8z PDB-2p8x PDB-2p8w EMDB-1364 PDB-3dny List of similar structure data about Omokage system

Article
Citation - primary
Article	Nature, Vol. 443, Issue 7112, Page 663-8, Year 2006
Title	Structure of eEF3 and the mechanism of transfer RNA release from the E-site.
Authors	Christian B F Andersen, Thomas Becker, Michael Blau, Monika Anand, Mario Halic, Bharvi Balar, Thorsten Mielke, Thomas Boesen, Jan Skov Pedersen, Christian M T Spahn, Terri Goss Kinzy, Gregers R Andersen, Roland Beckmann Centre for Structural Biology, Department of Molecular Biology, University of Aarhus, Gustav Wieds Vej 10C, DK-8000 Aarhus, Denmark.
Keywords	Adenosine Diphosphate (chemistry, 58-64-0), Adenosine Triphosphate (analogs & derivatives, 56-65-5), Binding Sites, Cryoelectron Microscopy, Crystallography, X-Ray, Fungal Proteins (chemistry), Gene Expression Regulation, Fungal, Models, Biological, Models, Molecular, Peptide Elongation Factors (chemistry), Protein Conformation, RNA, Transfer (metabolism, 9014-25-9), Ribosomes (chemistry), Saccharomyces cerevisiae (chemistry), Saccharomyces cerevisiae Proteins, Structure-Activity Relationship, YEF3 protein, S cerevisiae
Links	DOI: 10.1038/nature05126, PubMed: 16929303

Components
ID 1 : EF-3A, EF-3, TRANSLATION ELONGATION FACTOR 3A, EUKARYOTIC ELONGATION FACTOR 3, EEF3, YEAST ELONGATION FACTOR 3
Image
Description	ELONGATION FACTOR 3A
Type	polymer
Fragment	RESIDUES 1-976
Formula weight	109442.336 Da
Number of molecules	1
Details	TRANSLATION ELONGATION IN FUNGI ABC-TYPE ATPASE TRNA RELEASE
Source	Method: Isolated from a genetically manipulated source Gene: BAKER'S YEAST, ID:4932, SACCHAROMYCES CEREVISIAE Host: ID:4932, SACCHAROMYCES CEREVISIAE , WCGA Plasmid name: PYES2.1-TOPO
Links	UniProt: P16521, Sequence view

Sample
Assembly
Aggregation state	PARTICLE
Name	80S-RNC-EEF3-AMP-PNP COMPLEX
Buffer
Name	20MM HEPES,PH 7.5,10MM MG(OAC)2,150MM KOAC 1MM DTT,0.05% NIKKOL, 125MM SUCROSE,0.01MG -ML-1 CYCLOHEXIMIDE,0.5MM AMP-PNP,0.1MM NEOMYCIN, 0.3% DESOXYBIGCHAPS
Experiment
Reconstruction method	SINGLE PARTICLE
Specimen type	VITREOUS ICE (CRYO EM)
Sample preparation
pH	7.5
Sample concentration	0.17 mg/ml
Sample support
Details	HOLEY CARBON
Vitrification
Details	LIQUID ETHANE