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3U1M

Structure of the mRNA splicing complex component Cwc2

Summary for 3U1M
Entry DOI10.2210/pdb3u1m/pdb
Related3U1L
DescriptorPre-mRNA-splicing factor CWC2, ZINC ION (3 entities in total)
Functional Keywordscsmp, zinc finger, mrna splicing, splicing
Biological sourceSaccharomyces cerevisiae (Baker's yeast)
Cellular locationNucleus: Q12046
Total number of polymer chains1
Total formula weight27438.51
Authors
Lu, P.,Lu, G.,Yan, C.,Wang, L.,Li, W.,Yin, P. (deposition date: 2011-09-30, release date: 2011-11-16, Last modification date: 2023-11-01)
Primary citationLu, P.,Lu, G.,Yan, C.,Wang, L.,Li, W.,Yin, P.
Structure of the mRNA splicing complex component Cwc2: insights into RNA recognition
Biochem.J., 441:591-597, 2012
Cited by
PubMed Abstract: The Prp19-associated complex [NTC (nineteen complex)] plays a crucial role in intron removal during premature mRNA splicing in eukaryotes. Only one component of the NTC, Cwc2, is capable of binding RNA. In the present study we report the 1.9 Å (1 Å=0.1 nm) X-ray structure of the Cwc2 core domain, which is both necessary and sufficient for RNA binding. The Cwc2 core domain contains two sub-domains, a CCCH-type ZnF (zinc finger) and a RRM (RNA recognition motif). Unexpectedly, the ZnF domain and the RRM form a single folding unit, glued together by extensive hydrophobic interactions and hydrogen bonds. Structure-guided mutational analysis revealed that the intervening loop [known as the RB loop (RNA-binding loop)] between ZnF and RRM plays an essential role in RNA binding. In addition, a number of highly conserved positively charged residues on the β-strands of RRM make an important contribution to RNA binding. Intriguingly, these residues and a portion of the RB loop constitute an extended basic surface strip that encircles Cwc2 halfway. The present study serves as a framework for understanding the regulatory function of the NTC in RNA splicing.
PubMed: 21957909
DOI: 10.1042/BJ20111385
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.95 Å)
Structure validation

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数据于2024-10-30公开中

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