1hq1
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(New page: 200px<br /><applet load="1hq1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hq1, resolution 1.52Å" /> '''STRUCTURAL AND ENERG...)
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Revision as of 14:36, 20 November 2007
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STRUCTURAL AND ENERGETIC ANALYSIS OF RNA RECOGNITION BY A UNIVERSALLY CONSERVED PROTEIN FROM THE SIGNAL RECOGNITION PARTICLE
Overview
The signal recognition particle (SRP) is a ribonucleoprotein complex, responsible for targeting proteins to the endoplasmic reticulum in eukarya, or to the inner membrane in prokarya. The crystal structure of the, universally conserved RNA-protein core of the Escherichia coli SRP, refined here to 1.5 A resolution, revealed minor groove recognition of the, 4.5 S RNA component by the M domain of the Ffh protein. Within the RNA, nucleotides comprising two phylogenetically conserved internal loops, create a unique surface for protein recognition. To determine the, energetic importance of conserved nucleotides for SRP assembly, we, measured the affinity of the M domain for a series of RNA mutants. This, analysis reveals how conserved nucleotides within the two internal loop, motifs establish the architecture of the macromolecular interface and, position essential functional groups for direct recognition by the, protein.
About this Structure
1HQ1 is a Single protein structure of sequence from Escherichia coli with MG and K as ligands. Full crystallographic information is available from OCA.
Reference
Structural and energetic analysis of RNA recognition by a universally conserved protein from the signal recognition particle., Batey RT, Sagar MB, Doudna JA, J Mol Biol. 2001 Mar 16;307(1):229-46. PMID:11243816
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