3a1y
From Proteopedia
Contents |
The structure of archaeal ribosomal stalk P1/P0 complex
Template:ABSTRACT PUBMED 20007716
Function
[RL12_PYRHO] Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors. The stalk complex of P.horikoshii binds to E.coli large subunits and confers on them the ability to interact with eukaryotic elongation factors. Each succesive L12 dimer bound along the P0 spine increases the GTPase activity of elongation factors and increases translation by reconsituted ribosomes.[1] [RL10_PYRHO] Forms the large subunit's ribosomal stalk, playing a central role in the interaction of the ribosome with elongation factors; the stalk complex of P.horikoshii binds to E.coli large subunits and confers on them the ability to interact with eukaryotic elongation factors. Each succesive L12 dimer bound along the P0 spine increases the GTPase activity of elongation factors and increases translation by reconsituted ribosomes, although the first site is the most stimulatory.[2]
About this Structure
3a1y is a 7 chain structure with sequence from 'pyrococcus shinkaii'. Full crystallographic information is available from OCA.
See Also
Reference
- Naganuma T, Nomura N, Yao M, Mochizuki M, Uchiumi T, Tanaka I. Structural basis for translation factor recruitment to the eukaryotic/archaeal ribosomes. J Biol Chem. 2010 Feb 12;285(7):4747-56. Epub 2009 Dec 10. PMID:20007716 doi:10.1074/jbc.M109.068098
- ↑ Maki Y, Hashimoto T, Zhou M, Naganuma T, Ohta J, Nomura T, Robinson CV, Uchiumi T. Three binding sites for stalk protein dimers are generally present in ribosomes from archaeal organism. J Biol Chem. 2007 Nov 9;282(45):32827-33. Epub 2007 Sep 5. PMID:17804412 doi:http://dx.doi.org/10.1074/jbc.M705412200
- ↑ Maki Y, Hashimoto T, Zhou M, Naganuma T, Ohta J, Nomura T, Robinson CV, Uchiumi T. Three binding sites for stalk protein dimers are generally present in ribosomes from archaeal organism. J Biol Chem. 2007 Nov 9;282(45):32827-33. Epub 2007 Sep 5. PMID:17804412 doi:http://dx.doi.org/10.1074/jbc.M705412200