3bbo

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{{STRUCTURE_3bbo| PDB=3bbo | SCENE= }}
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'''Homology model for the Spinach chloroplast 50S subunit fitted to 9.4A cryo-EM map of the 70S chlororibosome'''
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===Homology model for the Spinach chloroplast 50S subunit fitted to 9.4A cryo-EM map of the 70S chlororibosome===
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==Overview==
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Protein synthesis in the chloroplast is carried out by chloroplast ribosomes (chloro-ribosome) and regulated in a light-dependent manner. Chloroplast or plastid ribosomal proteins (PRPs) generally are larger than their bacterial counterparts, and chloro-ribosomes contain additional plastid-specific ribosomal proteins (PSRPs); however, it is unclear to what extent these proteins play structural or regulatory roles during translation. We have obtained a three-dimensional cryo-EM map of the spinach 70S chloro-ribosome, revealing the overall structural organization to be similar to bacterial ribosomes. Fitting of the conserved portions of the x-ray crystallographic structure of the bacterial 70S ribosome into our cryo-EM map of the chloro-ribosome reveals the positions of PRP extensions and the locations of the PSRPs. Surprisingly, PSRP1 binds in the decoding region of the small (30S) ribosomal subunit, in a manner that would preclude the binding of messenger and transfer RNAs to the ribosome, suggesting that PSRP1 is a translation factor rather than a ribosomal protein. PSRP2 and PSRP3 appear to structurally compensate for missing segments of the 16S rRNA within the 30S subunit, whereas PSRP4 occupies a position buried within the head of the 30S subunit. One of the two PSRPs in the large (50S) ribosomal subunit lies near the tRNA exit site. Furthermore, we find a mass of density corresponding to chloro-ribosome recycling factor; domain II of this factor appears to interact with the flexible C-terminal domain of PSRP1. Our study provides evolutionary insights into the structural and functional roles that the PSRPs play during protein synthesis in chloroplasts.
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==About this Structure==
==About this Structure==
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[[Category: Ribonucleoprotein particle]]
[[Category: Ribonucleoprotein particle]]
[[Category: Spinach chloroplast ribosome]]
[[Category: Spinach chloroplast ribosome]]
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Revision as of 00:24, 28 July 2008

Image:3bbo.png

Template:STRUCTURE 3bbo

Homology model for the Spinach chloroplast 50S subunit fitted to 9.4A cryo-EM map of the 70S chlororibosome

Template:ABSTRACT PUBMED 18042701

About this Structure

3BBO is a Protein complex structure of sequences from Arabidopsis thaliana, Nicotiana tabacum, Pisum sativum, Spinacia oleracea and Vitis vinifera. Full crystallographic information is available from OCA.

Reference

Cryo-EM study of the spinach chloroplast ribosome reveals the structural and functional roles of plastid-specific ribosomal proteins., Sharma MR, Wilson DN, Datta PP, Barat C, Schluenzen F, Fucini P, Agrawal RK, Proc Natl Acad Sci U S A. 2007 Dec 4;104(49):19315-20. Epub 2007 Nov 27. PMID:18042701

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