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2i7x

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(New page: 200px<br /><applet load="2i7x" size="450" color="white" frame="true" align="right" spinBox="true" caption="2i7x, resolution 2.50&Aring;" /> '''Structure of Yeast C...)
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'''Structure of Yeast CPSF-100 (Ydh1p)'''<br />
'''Structure of Yeast CPSF-100 (Ydh1p)'''<br />
==Overview==
==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.
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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.
==About this Structure==
==About this Structure==
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2I7X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2I7X OCA].
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2I7X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2I7X OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Gebauer, D.]]
[[Category: Gebauer, D.]]
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[[Category: Mandel, C.R.]]
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[[Category: Mandel, C R.]]
[[Category: Tong, L.]]
[[Category: Tong, L.]]
[[Category: Zhang, H.]]
[[Category: Zhang, H.]]
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[[Category: v(d)j recombination]]
[[Category: v(d)j recombination]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 12:11:04 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:50:02 2008''

Revision as of 15:50, 21 February 2008


2i7x, resolution 2.50Å

Drag the structure with the mouse to rotate

Structure of Yeast CPSF-100 (Ydh1p)

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.

About this Structure

2I7X is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

Polyadenylation factor CPSF-73 is the pre-mRNA 3'-end-processing endonuclease., Mandel CR, Kaneko S, Zhang H, Gebauer D, Vethantham V, Manley JL, Tong L, Nature. 2006 Dec 14;444(7121):953-6. Epub 2006 Nov 26. PMID:17128255

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