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| {{STRUCTURE_2i7t| PDB=2i7t | SCENE= }} | | {{STRUCTURE_2i7t| PDB=2i7t | SCENE= }} |
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| '''Structure of human CPSF-73'''
| | ===Structure of human CPSF-73=== |
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| ==Overview==
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| Most eukaryotic messenger RNA precursors (pre-mRNAs) undergo extensive maturational processing, including cleavage and polyadenylation at the 3'-end. Despite the characterization of many proteins that are required for the cleavage reaction, the identity of the endonuclease is not known. Recent analyses indicated that the 73-kDa subunit of cleavage and polyadenylation specificity factor (CPSF-73) might be the endonuclease for this and related reactions, although no direct data confirmed this. Here we report the crystal structures of human CPSF-73 at 2.1 A resolution, complexed with zinc ions and a sulphate that might mimic the phosphate group of the substrate, and the related yeast protein CPSF-100 (Ydh1) at 2.5 A resolution. Both CPSF-73 and CPSF-100 contain two domains, a metallo-beta-lactamase domain and a novel beta-CASP (named for metallo-beta-lactamase, CPSF, Artemis, Snm1, Pso2) domain. The active site of CPSF-73, with two zinc ions, is located at the interface of the two domains. Purified recombinant CPSF-73 possesses RNA endonuclease activity, and mutations that disrupt zinc binding in the active site abolish this activity. Our studies provide the first direct experimental evidence that CPSF-73 is the pre-mRNA 3'-end-processing endonuclease.
| | The line below this paragraph, {{ABSTRACT_PUBMED_17128255}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17128255 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_17128255}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Polyadenylation]] | | [[Category: Polyadenylation]] |
| [[Category: Pre-mrna processing]] | | [[Category: Pre-mrna processing]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 07:11:09 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 07:11:17 2008'' |
