4J7N
Crystal structure of mouse DXO in complex with M7GPPPG cap
Summary for 4J7N
Entry DOI | 10.2210/pdb4j7n/pdb |
Related | 3FQI 3FQJ 4J7L 4J7M |
Descriptor | Protein Dom3Z, 7-METHYL-GUANOSINE-5'-TRIPHOSPHATE-5'-GUANOSINE, 9-METHYLGUANINE, ... (5 entities in total) |
Functional Keywords | decapping, 5'-3' exoribonuclease, hydrolase |
Biological source | Mus musculus (mouse) |
Cellular location | Nucleus (By similarity): O70348 |
Total number of polymer chains | 1 |
Total formula weight | 45028.70 |
Authors | Kilic, T.,Chang, J.H.,Tong, L. (deposition date: 2013-02-13, release date: 2013-03-27, Last modification date: 2024-02-28) |
Primary citation | Jiao, X.,Chang, J.H.,Kilic, T.,Tong, L.,Kiledjian, M. A mammalian pre-mRNA 5' end capping quality control mechanism and an unexpected link of capping to pre-mRNA processing. Mol.Cell, 50:104-115, 2013 Cited by PubMed Abstract: Recently, we reported that two homologous yeast proteins, Rai1 and Dxo1, function in a quality control mechanism to clear cells of incompletely 5' end-capped messenger RNAs (mRNAs). Here, we report that their mammalian homolog, Dom3Z (referred to as DXO), possesses pyrophosphohydrolase, decapping, and 5'-to-3' exoribonuclease activities. Surprisingly, we found that DXO preferentially degrades defectively capped pre-mRNAs in cells. Additional studies show that incompletely capped pre-mRNAs are inefficiently spliced at all introns, a fact that contrasts with current understanding, and are also poorly cleaved for polyadenylation. Crystal structures of DXO in complex with substrate mimic and products at a resolution of up to 1.5Å provide elegant insights into the catalytic mechanism and molecular basis for their three apparently distinct activities. Our data reveal a pre-mRNA 5' end capping quality control mechanism in mammalian cells, indicating DXO as the central player for this mechanism, and demonstrate an unexpected intimate link between proper 5' end capping and subsequent pre-mRNA processing. PubMed: 23523372DOI: 10.1016/j.molcel.2013.02.017 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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