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1v8q

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(New page: 200px<br /><applet load="1v8q" size="450" color="white" frame="true" align="right" spinBox="true" caption="1v8q, resolution 2.80&Aring;" /> '''Crystal structure of...)
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Revision as of 19:42, 24 November 2007

Image:1v8q.gif

1v8q, resolution 2.80Å

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Crystal structure of ribosomal protein L27 from Thermus thermophilus HB8

Overview

Ribosomal protein L27 is located near the peptidyltransferase center at, the interface of ribosomal subunits, and is important for ribosomal, assembly and function. We report the crystal structure of ribosomal, protein L27 from Thermus thermophilus HB8, which was determined by the, multiwavelength anomalous dispersion method and refined to an R-factor of, 19.7% (R(free) = 23.6%) at 2.8 A resolution. The overall fold is an all, beta-sheet hybrid. It consists of two sets of four-stranded beta-sheets, formed around a well-defined hydrophobic core, with a highly positive, charge on the protein surface. The structure of ribosomal protein L27 from, T. thermophilus HB8 in the RNA-free form is investigated, and its, functional roles in the ribosomal subunit are discussed.

About this Structure

1V8Q is a Single protein structure of sequence from Thermus thermophilus with DTT as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structure of ribosomal protein L27 from Thermus thermophilus HB8., Wang H, Takemoto CH, Murayama K, Sakai H, Tatsuguchi A, Terada T, Shirouzu M, Kuramitsu S, Yokoyama S, Protein Sci. 2004 Oct;13(10):2806-10. Epub 2004 Aug 31. PMID:15340170

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