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| [[Image:1xtk.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1xtk| PDB=1xtk | SCENE= }} | | {{STRUCTURE_1xtk| PDB=1xtk | SCENE= }} |
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| '''structure of DECD to DEAD mutation of human UAP56'''
| | ===structure of DECD to DEAD mutation of human UAP56=== |
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| ==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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_15585580}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 15585580 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_15585580}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Xu, R M.]] | | [[Category: Xu, R M.]] |
| [[Category: Alpha-beta fold]] | | [[Category: Alpha-beta fold]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:29:37 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 16:33:45 2008'' |
