1C04

IDENTIFICATION OF KNOWN PROTEIN AND RNA STRUCTURES IN A 5 A MAP OF THE LARGE RIBOSOMAL SUBUNIT FROM HALOARCULA MARISMORTUI

Summary for 1C04

• Entry DOI: 10.2210/pdb1c04/pdb
• Related: 1QA6 1RL2 1RL6 1WHI 430D
• Descriptor: 23S RRNA FRAGMENT, RIBOSOMAL PROTEIN L2, RIBOSOMAL PROTEIN L6, ... (6 entities in total)
• Functional Keywords: low resolution model, large ribosome unit, ribosome
• Biological source: Haloarcula marismortui; More
• Total number of polymer chains: 6
• Total formula weight: 82720.78

Authors

Ban, N.,Nissen, P.,Capel, M.,Moore, P.B.,Steitz, T.A. (deposition date: 1999-07-14, release date: 1999-08-31, Last modification date: 2024-10-30)

Primary citation

Ban, N.,Nissen, P.,Hansen, J.,Capel, M.,Moore, P.B.,Steitz, T.A.
Placement of protein and RNA structures into a 5 A-resolution map of the 50S ribosomal subunit.
Nature, 400:841-847, 1999

PubMed Abstract: We have calculated at 5.0 A resolution an electron-density map of the large 50S ribosomal subunit from the bacterium Haloarcula marismortui by using phases derived from four heavy-atom derivatives, intercrystal density averaging and density-modification procedures. More than 300 base pairs of A-form RNA duplex have been fitted into this map, as have regions of non-A-form duplex, single-stranded segments and tetraloops. The long rods of RNA crisscrossing the subunit arise from the stacking of short, separate double helices, not all of which are A-form, and in many places proteins crosslink two or more of these rods. The polypeptide exit channel was marked by tungsten cluster compounds bound in one heavy-atom-derivatized crystal. We have determined the structure of the translation-factor-binding centre by fitting the crystal structures of the ribosomal proteins L6, L11 and L14, the sarcin-ricin loop RNA, and the RNA sequence that binds L11 into the electron density. We can position either elongation factor G or elongation factor Tu complexed with an aminoacylated transfer RNA and GTP onto the factor-binding centre in a manner that is consistent with results from biochemical and electron microscopy studies.

PubMed: 10476961
DOI: 10.1038/23641

Experimental method

X-RAY DIFFRACTION (5 Å)