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The | ==CRYSTAL STRUCTURE OF THE DEAH-BOX HELICASE PRP2 IN COMPLEX WITH ADP== | ||
<StructureSection load='6fac' size='340' side='right' caption='[[6fac]], [[Resolution|resolution]] 2.05Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6fac]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FAC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6FAC 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=CL:CHLORIDE+ION'>CL</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=6fac FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fac OCA], [http://pdbe.org/6fac PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6fac RCSB], [http://www.ebi.ac.uk/pdbsum/6fac PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6fac ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The DEAH-box ATPase Prp2 plays a key role in the activation of the spliceosome as it promotes the transition from the B(act) to the catalytically active B* spliceosome. Here, four crystal structures of Prp2 are reported: one of the nucleotide-free state and three different structures of the ADP-bound state. The overall conformation of the helicase core, formed by two RecA-like domains, does not differ significantly between the ADP-bound and the nucleotide-free states. However, intrinsic flexibility of Prp2 is observed, varying the position of the C-terminal domains with respect to the RecA domains. Additionally, in one of the structures a unique ADP conformation is found which has not been observed in any other DEAH-box, DEAD-box or NS3/NPH-II helicase. | |||
Crystal structure of the spliceosomal DEAH-box ATPase Prp2.,Schmitt A, Hamann F, Neumann P, Ficner R Acta Crystallogr D Struct Biol. 2018 Jul 1;74(Pt 7):643-654. doi:, 10.1107/S2059798318006356. Epub 2018 Jun 8. PMID:29968674<ref>PMID:29968674</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6fac" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Ficner, R]] | |||
[[Category: Hamann, F]] | [[Category: Hamann, F]] | ||
[[Category: Neumann, P]] | [[Category: Neumann, P]] | ||
[[Category: Schmitt, A]] | [[Category: Schmitt, A]] | ||
[[Category: Atpase]] | |||
[[Category: G-patch]] | |||
[[Category: Helicase]] | |||
[[Category: Hydrolase]] | |||
[[Category: Splicing]] |
Revision as of 08:46, 11 July 2018
CRYSTAL STRUCTURE OF THE DEAH-BOX HELICASE PRP2 IN COMPLEX WITH ADPCRYSTAL STRUCTURE OF THE DEAH-BOX HELICASE PRP2 IN COMPLEX WITH ADP
Structural highlights
Publication Abstract from PubMedThe DEAH-box ATPase Prp2 plays a key role in the activation of the spliceosome as it promotes the transition from the B(act) to the catalytically active B* spliceosome. Here, four crystal structures of Prp2 are reported: one of the nucleotide-free state and three different structures of the ADP-bound state. The overall conformation of the helicase core, formed by two RecA-like domains, does not differ significantly between the ADP-bound and the nucleotide-free states. However, intrinsic flexibility of Prp2 is observed, varying the position of the C-terminal domains with respect to the RecA domains. Additionally, in one of the structures a unique ADP conformation is found which has not been observed in any other DEAH-box, DEAD-box or NS3/NPH-II helicase. Crystal structure of the spliceosomal DEAH-box ATPase Prp2.,Schmitt A, Hamann F, Neumann P, Ficner R Acta Crystallogr D Struct Biol. 2018 Jul 1;74(Pt 7):643-654. doi:, 10.1107/S2059798318006356. Epub 2018 Jun 8. PMID:29968674[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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