1914

From Proteopedia

Revision as of 13:37, 5 November 2007

SIGNAL RECOGNITION PARTICLE ALU RNA BINDING HETERODIMER, SRP9/14

Overview

The mammalian signal recognition particle (SRP) is an 11S cytoplasmic, ribonucleoprotein that plays an essential role in protein sorting. SRP, recognizes the signal sequence of the nascent polypeptide chain emerging, from the ribosome, and targets the ribosome-nascent chain-SRP complex to, the rough endoplasmic reticulum. The SRP consists of six polypeptides, (SRP9, SRP14, SRP19, SRP54, SRP68 and SRP72) and a single 300 nucleotide, RNA molecule. SRP9 and SRP14 proteins form a heterodimer that binds to the, Alu domain of SRP RNA which is responsible for translation arrest. We, report the first crystal structure of a mammalian SRP protein, that of the, mouse SRP9/14 heterodimer, determined at 2.5 A resolution. SRP9 and SRP14, are found to be structurally homologous, containing the same, alpha-beta-beta-beta-alpha fold. This we designate the Alu binding module, (Alu bm), an additional member of the family of small alpha/beta RNA, binding domains. The heterodimer has pseudo 2-fold symmetry and is saddle, like, comprising a strongly curved six-stranded amphipathic beta-sheet, with the four helices packed on the convex side and the exposed concave, surface being lined with positively charged residues.

About this Structure

1914 is a Single protein structure of sequence from Mus musculus with PO4 and BME as ligands. Structure known Active Site: NUL. Full crystallographic information is available from OCA.

Reference

The crystal structure of the signal recognition particle Alu RNA binding heterodimer, SRP9/14., Birse DE, Kapp U, Strub K, Cusack S, Aberg A, EMBO J. 1997 Jul 1;16(13):3757-66. PMID:9233785

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