2i7v: Difference between revisions

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==Overview==

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.

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.

==About this Structure==

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[[Category: Homo sapiens]]

[[Category: Single protein]]

[[Category: Mandel, C.R.]]

[[Category: Mandel, C R.]]

[[Category: Tong, L.]]

[[Category: Zhang, H.]]

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[[Category: v(d)j recombination]]

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@@ Line 4: / Line 4: @@
 ==Overview==
-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.
+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.
 ==About this Structure==
@@ Line 13: / Line 13: @@
 [[Category: Homo sapiens]]
 [[Category: Single protein]]
-[[Category: Mandel, C.R.]]
+[[Category: Mandel, C R.]]
 [[Category: Tong, L.]]
 [[Category: Zhang, H.]]
@@ Line 25: / Line 25: @@
 [[Category: v(d)j recombination]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 17:35:15 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:49:58 2008''