1qgv
From Proteopedia
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HUMAN SPLICEOSOMAL PROTEIN U5-15KD
Overview
The U5 small ribonucleoprotein particle (snRNP) contains various proteins, involved in catalytic activities mediating conformational rearrangements, of the spliceosome. We have isolated and characterized the evolutionarily, highly conserved human U5 snRNP-specific protein U5-15kD. The crystal, structure of U5-15kD determined at 1.4 A resolution revealed a, thioredoxin-like fold and represents the first structure of a U5, snRNP-specific protein known so far. With respect to human thioredoxin the, U5-15kD protein contains 37 additional residues causing structural changes, which most likely form putative binding sites for other spliceosomal, proteins or RNA. Moreover, a novel intramolecular disulfide bond replaces, the canonical one found in the thioredoxin family. Even though U5-15kD, appears to lack protein disulfide isomerase activity, it is strictly, required for pre-mRNA splicing in vivo as we demonstrate by genetic, depletion of its ortholog in Saccharomyces cerevisiae. Our data suggest, that the previously reported involvement of its Schizosaccharomyces pombe, ortholog Dim1p in cell cycle regulation is a consequence of its essential, role in pre-mRNA splicing.
About this Structure
1QGV is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Identification, characterization and crystal structure analysis of the human spliceosomal U5 snRNP-specific 15 kD protein., Reuter K, Nottrott S, Fabrizio P, Luhrmann R, Ficner R, J Mol Biol. 1999 Nov 26;294(2):515-25. PMID:10610776
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