3bbo: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
New page: left|200px <!-- The line below this paragraph, containing "STRUCTURE_3bbo", creates the "Structure Box" on the page. You may change the PDB parameter (which sets the PD...
 
OCA (talk | contribs)
No edit summary
Line 1: Line 1:
[[Image:3bbo.jpg|left|200px]]
{{Seed}}
[[Image:3bbo.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_3bbo|  PDB=3bbo  |  SCENE=  }}  
{{STRUCTURE_3bbo|  PDB=3bbo  |  SCENE=  }}  


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




==Overview==
<!--  
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.
The line below this paragraph, {{ABSTRACT_PUBMED_18042701}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 18042701 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_18042701}}


==About this Structure==
==About this Structure==
Line 37: Line 41:
[[Category: Ribonucleoprotein particle]]
[[Category: Ribonucleoprotein particle]]
[[Category: Spinach chloroplast ribosome]]
[[Category: Spinach chloroplast ribosome]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 28 09:19:16 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 03:24:18 2008''