5dtu: Difference between revisions
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==Crystal structure of the RNA-helicase Prp28 from Chaetomium thermophilum bound to ADP== | |||
<StructureSection load='5dtu' size='340' side='right' caption='[[5dtu]], [[Resolution|resolution]] 3.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5dtu]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DTU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DTU FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5dtu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dtu OCA], [http://pdbe.org/5dtu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dtu RCSB], [http://www.ebi.ac.uk/pdbsum/5dtu PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Prp28 (pre-mRNA-splicing ATP-dependent RNA helicase 28) is a spliceosomal DEAD-box helicase which is involved in two steps of spliceosome assembly. It is required for the formation of commitment complex 2 in an ATP-independent manner as well as for the formation of the pre-catalytic spliceosome, which in contrast is ATP-dependent. During the latter step, Prp28 is crucial for the integration of the U4/U6.U5 tri-snRNP since it displaces the U1 snRNP and allows the U6 snRNP to base-pair with the 5'-splice site. Here, the crystal structure of Prp28 from the thermophilic fungus Chaetomium thermophilum is reported at 3.2 A resolution and is compared with the available structures of homologues. | |||
Structural analysis of the spliceosomal RNA helicase Prp28 from the thermophilic eukaryote Chaetomium thermophilum.,Tauchert MJ, Ficner R Acta Crystallogr F Struct Biol Commun. 2016 May 1;72(Pt 5):409-16. doi:, 10.1107/S2053230X16006038. Epub 2016 Apr 22. PMID:27139834<ref>PMID:27139834</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5dtu" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Ficner, R]] | [[Category: Ficner, R]] | ||
[[Category: Tauchert, M J]] | |||
[[Category: Atpase]] | |||
[[Category: Ddx23]] | |||
[[Category: Dead-box protein]] | |||
[[Category: Hydrolase]] | |||
[[Category: Rna-helicase]] | |||
Revision as of 08:29, 11 May 2016
Crystal structure of the RNA-helicase Prp28 from Chaetomium thermophilum bound to ADPCrystal structure of the RNA-helicase Prp28 from Chaetomium thermophilum bound to ADP
Structural highlights
Publication Abstract from PubMedPrp28 (pre-mRNA-splicing ATP-dependent RNA helicase 28) is a spliceosomal DEAD-box helicase which is involved in two steps of spliceosome assembly. It is required for the formation of commitment complex 2 in an ATP-independent manner as well as for the formation of the pre-catalytic spliceosome, which in contrast is ATP-dependent. During the latter step, Prp28 is crucial for the integration of the U4/U6.U5 tri-snRNP since it displaces the U1 snRNP and allows the U6 snRNP to base-pair with the 5'-splice site. Here, the crystal structure of Prp28 from the thermophilic fungus Chaetomium thermophilum is reported at 3.2 A resolution and is compared with the available structures of homologues. Structural analysis of the spliceosomal RNA helicase Prp28 from the thermophilic eukaryote Chaetomium thermophilum.,Tauchert MJ, Ficner R Acta Crystallogr F Struct Biol Commun. 2016 May 1;72(Pt 5):409-16. doi:, 10.1107/S2053230X16006038. Epub 2016 Apr 22. PMID:27139834[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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