1xtk

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(New page: 200px<br /> <applet load="1xtk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xtk, resolution 2.40&Aring;" /> '''structure of DECD t...)
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[[Image:1xtk.gif|left|200px]]<br />
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[[Image:1xtk.gif|left|200px]]<br /><applet load="1xtk" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="1xtk" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1xtk, resolution 2.40&Aring;" />
caption="1xtk, resolution 2.40&Aring;" />
'''structure of DECD to DEAD mutation of human UAP56'''<br />
'''structure of DECD to DEAD mutation of human UAP56'''<br />
==Overview==
==Overview==
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Pre-mRNA splicing requires the function of a number of RNA-dependent, ATPases/helicases, yet no three-dimensional structure of any spliceosomal, ATPases/helicases is known. The highly conserved DECD-box protein, UAP56/Sub2 is an essential splicing factor that is also important for mRNA, export. The expected ATPase/helicase activity appears to be essential for, the UAP56/Sub2 functions. Here, we show that purified human UAP56 is an, active RNA-dependent ATPase, and we also report the crystal structures of, UAP56 alone and in complex with ADP, as well as a DECD to DEAD mutant. The, structures reveal a unique spatial arrangement of the two conserved, helicase domains, and ADP-binding induces significant conformational, changes of key residues in the ATP-binding pocket. Our structural analyses, suggest a specific protein-RNA displacement model of UAP56/Sub2. The, detailed structural information provides important mechanistic insights, into the splicing function of UAP56/Sub2. The structures also will be, useful for the analysis of other spliceosomal DExD-box ATPases/helicases.
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Pre-mRNA splicing requires the function of a number of RNA-dependent ATPases/helicases, yet no three-dimensional structure of any spliceosomal ATPases/helicases is known. The highly conserved DECD-box protein UAP56/Sub2 is an essential splicing factor that is also important for mRNA export. The expected ATPase/helicase activity appears to be essential for the UAP56/Sub2 functions. Here, we show that purified human UAP56 is an active RNA-dependent ATPase, and we also report the crystal structures of UAP56 alone and in complex with ADP, as well as a DECD to DEAD mutant. The structures reveal a unique spatial arrangement of the two conserved helicase domains, and ADP-binding induces significant conformational changes of key residues in the ATP-binding pocket. Our structural analyses suggest a specific protein-RNA displacement model of UAP56/Sub2. The detailed structural information provides important mechanistic insights into the splicing function of UAP56/Sub2. The structures also will be useful for the analysis of other spliceosomal DExD-box ATPases/helicases.
==About this Structure==
==About this Structure==
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1XTK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with BME as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1XTK OCA].
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1XTK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=BME:'>BME</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XTK OCA].
==Reference==
==Reference==
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[[Category: Cordin, O.]]
[[Category: Cordin, O.]]
[[Category: Linder, P.]]
[[Category: Linder, P.]]
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[[Category: Minder, C.M.]]
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[[Category: Minder, C M.]]
[[Category: Shi, H.]]
[[Category: Shi, H.]]
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[[Category: Xu, R.M.]]
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[[Category: Xu, R M.]]
[[Category: BME]]
[[Category: BME]]
[[Category: alpha-beta fold]]
[[Category: alpha-beta fold]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:10:42 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:58:37 2008''

Revision as of 13:58, 21 February 2008

Image:1xtk.gif

1xtk, resolution 2.40Å

Drag the structure with the mouse to rotate

structure of DECD to DEAD mutation of human UAP56

Overview

Pre-mRNA splicing requires the function of a number of RNA-dependent ATPases/helicases, yet no three-dimensional structure of any spliceosomal ATPases/helicases is known. The highly conserved DECD-box protein UAP56/Sub2 is an essential splicing factor that is also important for mRNA export. The expected ATPase/helicase activity appears to be essential for the UAP56/Sub2 functions. Here, we show that purified human UAP56 is an active RNA-dependent ATPase, and we also report the crystal structures of UAP56 alone and in complex with ADP, as well as a DECD to DEAD mutant. The structures reveal a unique spatial arrangement of the two conserved helicase domains, and ADP-binding induces significant conformational changes of key residues in the ATP-binding pocket. Our structural analyses suggest a specific protein-RNA displacement model of UAP56/Sub2. The detailed structural information provides important mechanistic insights into the splicing function of UAP56/Sub2. The structures also will be useful for the analysis of other spliceosomal DExD-box ATPases/helicases.

About this Structure

1XTK is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structure of the human ATP-dependent splicing and export factor UAP56., Shi H, Cordin O, Minder CM, Linder P, Xu RM, Proc Natl Acad Sci U S A. 2004 Dec 21;101(51):17628-33. Epub 2004 Dec 7. PMID:15585580

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