1dul
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(New page: 200px<br /><applet load="1dul" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dul, resolution 1.80Å" /> '''STRUCTURE OF THE RIB...)
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Revision as of 11:28, 20 November 2007
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STRUCTURE OF THE RIBONUCLEOPROTEIN CORE OF THE E. COLI SIGNAL RECOGNITION PARTICLE
Overview
The signal recognition particle (SRP), a protein-RNA complex conserved in, all three kingdoms of life, recognizes and transports specific proteins to, cellular membranes for insertion or secretion. We describe here the 1.8, angstrom crystal structure of the universal core of the SRP, revealing, protein recognition of a distorted RNA minor groove. Nucleotide analog, interference mapping demonstrates the biological importance of observed, interactions, and genetic results show that this core is functional in, vivo. The structure explains why the conserved residues in the protein and, RNA are required for SRP assembly and defines a signal sequence, recognition surface composed of both protein and RNA.
About this Structure
1DUL is a Protein complex structure of sequences from Escherichia coli with K and MG as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of the ribonucleoprotein core of the signal recognition particle., Batey RT, Rambo RP, Lucast L, Rha B, Doudna JA, Science. 2000 Feb 18;287(5456):1232-9. PMID:10678824
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