2wh1
From Proteopedia
Contents |
INSIGHTS INTO TRANSLATIONAL TERMINATION FROM THE STRUCTURE OF RF2 BOUND TO THE RIBOSOME
Template:ABSTRACT PUBMED 18988853
About this Structure
2wh1 is a 25 chain structure of Kink-turn motif, Ribosomal protein S10, Ribosomal protein S11, Ribosomal protein S12, Ribosomal protein S13, Ribosomal protein S14, Ribosomal protein S15, Ribosomal protein S16, Ribosomal protein S17, Ribosomal protein S18, Ribosomal protein S19, Ribosomal protein S2, Ribosomal protein S20, Ribosomal protein S3, Ribosomal protein S4, Ribosomal protein S5, Ribosomal protein S6, Ribosomal protein S7, Ribosomal protein S8, Ribosomal protein S9, Ribosomal protein THX and User:Wayne Decatur/kink-turn motif with sequence from Escherichia coli and Thermus thermophilus. This structure supersedes the now removed PDB entry 2jl5. Full crystallographic information is available from OCA.
See Also
- Kink-turn motif
- Ribosomal protein S10
- Ribosomal protein S11
- Ribosomal protein S12
- Ribosomal protein S13
- Ribosomal protein S14
- Ribosomal protein S15
- Ribosomal protein S16
- Ribosomal protein S17
- Ribosomal protein S18
- Ribosomal protein S19
- Ribosomal protein S2
- Ribosomal protein S20
- Ribosomal protein S3
- Ribosomal protein S4
- Ribosomal protein S5
- Ribosomal protein S6
- Ribosomal protein S7
- Ribosomal protein S8
- Ribosomal protein S9
- Ribosomal protein THX
- User:Wayne Decatur/kink-turn motif
Reference
- Weixlbaumer A, Jin H, Neubauer C, Voorhees RM, Petry S, Kelley AC, Ramakrishnan V. Insights into translational termination from the structure of RF2 bound to the ribosome. Science. 2008 Nov 7;322(5903):953-6. PMID:18988853 doi:http://dx.doi.org/322/5903/953
Categories: Escherichia coli | Thermus thermophilus | Jin, H. | Kelley, A C. | Neubauer, C. | Petry, S. | Ramakrishnan, V. | Voorhees, R M. | Weixlbaumer, A. | Metal-binding | Mrna | Protein biosynthesis | Rf2 | Ribonucleoprotein | Ribosomal protein | Ribosome | Rna-binding | Rrna-binding | Termination | Translation | Trna | Trna-binding | Zinc-finger
