4lk2
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4lk2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LK2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LK2 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4lk2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LK2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LK2 FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.12Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4lk2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lk2 OCA], [https://pdbe.org/4lk2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lk2 RCSB], [https://www.ebi.ac.uk/pdbsum/4lk2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lk2 ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4lk2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lk2 OCA], [https://pdbe.org/4lk2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lk2 RCSB], [https://www.ebi.ac.uk/pdbsum/4lk2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lk2 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/PRP5_YEAST PRP5_YEAST] ATP-dependent RNA helicase involved spliceosome assembly and in nuclear splicing. Catalyzes an ATP-dependent conformational change of U2 snRNP. Bridges U1 and U2 snRNPs and enables stable U2 snRNP association with intron RNA.<ref>PMID:8405998</ref> <ref>PMID:8065365</ref> <ref>PMID:8969184</ref> <ref>PMID:8969185</ref> <ref>PMID:8622683</ref> <ref>PMID:11927574</ref> <ref>PMID:14610285</ref> <ref>PMID:16314500</ref> | [https://www.uniprot.org/uniprot/PRP5_YEAST PRP5_YEAST] ATP-dependent RNA helicase involved spliceosome assembly and in nuclear splicing. Catalyzes an ATP-dependent conformational change of U2 snRNP. Bridges U1 and U2 snRNPs and enables stable U2 snRNP association with intron RNA.<ref>PMID:8405998</ref> <ref>PMID:8065365</ref> <ref>PMID:8969184</ref> <ref>PMID:8969185</ref> <ref>PMID:8622683</ref> <ref>PMID:11927574</ref> <ref>PMID:14610285</ref> <ref>PMID:16314500</ref> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The DEAD-box adenosine triphosphatase (ATPase) Prp5p facilitates U2 small nuclear ribonucleoprotein particle (snRNP) binding to the intron branch site region during spliceosome assembly. We present crystal structures of S. cerevisiae Prp5p alone and in complex with ADP at 2.12 A and 1.95 A resolution. The three-dimensional packing of Prp5p subdomains differs strikingly from that so far observed in other DEAD-box proteins: two RecA-like subdomains adopt an "open state" conformation stabilized by extensive interactions involving sequences that flank the two subdomains. This conformation is distinct from that required for ATP hydrolysis. Consistent with this, Prp5p mutations that destabilize interdomain interactions exhibited increased ATPase activity in vitro and inhibited splicing of suboptimal branch site substrates in vivo, whereas restoration of interdomain interactions reversed these effects. We conclude that the Prp5p open state conformation is biologically relevant and that disruption of the interdomain interaction facilitates a large-scale conformational change of Prp5p during U2 snRNP-branch site recognition. | ||
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| - | Crystal structure of Prp5p reveals interdomain interactions that impact spliceosome assembly.,Zhang ZM, Yang F, Zhang J, Tang Q, Li J, Gu J, Zhou J, Xu YZ Cell Rep. 2013 Dec 12;5(5):1269-78. doi: 10.1016/j.celrep.2013.10.047. Epub 2013 , Nov 27. PMID:24290758<ref>PMID:24290758</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 4lk2" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
Crystal structure of RNA splicing effector Prp5
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