1c04
From Proteopedia
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IDENTIFICATION OF KNOWN PROTEIN AND RNA STRUCTURES IN A 5 A MAP OF THE LARGE RIBOSOMAL SUBUNIT FROM HALOARCULA MARISMORTUI
Overview
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.
About this Structure
1C04 is a Protein complex structure of sequences from Haloarcula marismortui. Full crystallographic information is available from OCA.
Reference
Placement of protein and RNA structures into a 5 A-resolution map of the 50S ribosomal subunit., Ban N, Nissen P, Hansen J, Capel M, Moore PB, Steitz TA, Nature. 1999 Aug 26;400(6747):841-7. PMID:10476961
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