28sp
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(New page: 200px<br /><applet load="28sp" size="350" color="white" frame="true" align="right" spinBox="true" caption="28sp" /> '''NMR STRUCTURE OF THE MOST CONSERVED RNA MOTI...)
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Revision as of 15:50, 29 January 2008
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NMR STRUCTURE OF THE MOST CONSERVED RNA MOTIF IN SRP RNA
Overview
The signal recognition particle (SRP) directs translating ribosomes to the, protein translocation apparatus of endoplasmic reticulum (ER) membrane or, the bacterial plasma membrane. The SRP is universally conserved, and in, prokaryotes consists of two essential subunits, SRP RNA and SRP54, the, latter of which binds to signal sequences on the nascent protein chains., Here we describe the solution NMR structure of a 28-mer RNA composing the, most conserved part of SRP RNA to which SRP54 binds. Central to this, function is a six-nucleotide internal loop that assumes a novel, Mg2+-dependent structure with unusual cross-strand interactions; besides a, cross-strand A/A stack, two guanines form hydrogen bonds with, opposite-strand phosphates. The structure completely explains the, phylogenetic conservation of the loop bases, underlining its importance, for SRP54 binding and SRP function.
About this Structure
28SP is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Structure of the most conserved internal loop in SRP RNA., Schmitz U, James TL, Lukavsky P, Walter P, Nat Struct Biol. 1999 Jul;6(7):634-8. PMID:10404218
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