1QGV

HUMAN SPLICEOSOMAL PROTEIN U5-15KD

1QGV の概要

• エントリーDOI: 10.2210/pdb1qgv/pdb
• 分子名称: SPLICEOSOMAL PROTEIN U5-15KD (2 entities in total)
• 機能のキーワード: spliceosomal protein, snrnp, thioredoxin, transcription
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 16807.35

構造登録者

Reuter, K.,Nottrott, S.,Fabrizio, P.,Luehrmann, R.,Ficner, R. (登録日: 1999-05-06, 公開日: 1999-12-12, 最終更新日: 2024-10-30)

主引用文献

Reuter, K.,Nottrott, S.,Fabrizio, P.,Luhrmann, R.,Ficner, R.
Identification, characterization and crystal structure analysis of the human spliceosomal U5 snRNP-specific 15 kD protein.
J.Mol.Biol., 294:515-525, 1999

PubMed Abstract: 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.

PubMed: 10610776
DOI: 10.1006/jmbi.1999.3258

実験手法

X-RAY DIFFRACTION (1.4 Å)