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5EWR

C merolae U4 snRNP protein Snu13

Summary for 5EWR
Entry DOI10.2210/pdb5ewr/pdb
DescriptorBox C/D snoRNP and U4 snRNP component Snu13p (2 entities in total)
Functional Keywordssplicing, rna binding protein
Biological sourceCyanidioschyzon merolae (Red alga)
Total number of polymer chains1
Total formula weight15790.30
Authors
Garside, E.L.,Black, C.,Rader, S.,MacMillan, A.M. (deposition date: 2015-11-20, release date: 2016-04-20, Last modification date: 2023-09-27)
Primary citationBlack, C.S.,Garside, E.L.,MacMillan, A.M.,Rader, S.D.
Conserved structure of Snu13 from the highly reduced spliceosome of Cyanidioschyzon merolae.
Protein Sci., 25:911-916, 2016
Cited by
PubMed Abstract: Structural and functional analysis of proteins involved in pre-mRNA splicing is challenging because of the complexity of the splicing machinery, known as the spliceosome. Bioinformatic, proteomic, and biochemical analyses have identified a minimal spliceosome in the red alga Cyanidioschyzon merolae. This spliceosome consists of only 40 core proteins, compared to ∼ 70 in S. cerevisiae (yeast) and ∼ 150 in humans. We report the X-ray crystallographic analysis of C. merolae Snu13 (CmSnu13), a key component of the assembling spliceosome, and present evidence for conservation of Snu13 function in this algal splicing pathway. The near identity of CmSnu13's three-dimensional structure to yeast and human Snu13 suggests that C. merolae should be an excellent model system for investigating the structure and function of the conserved core of the spliceosome.
PubMed: 26833716
DOI: 10.1002/pro.2894
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.35 Å)
Structure validation

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