5ltk: Difference between revisions
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<StructureSection load='5ltk' size='340' side='right'caption='[[5ltk]], [[Resolution|resolution]] 3.24Å' scene=''> | <StructureSection load='5ltk' size='340' side='right'caption='[[5ltk]], [[Resolution|resolution]] 3.24Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5ltk]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5ltk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Chaetomium_thermophilum_var._thermophilum_DSM_1495 Chaetomium thermophilum var. thermophilum DSM 1495]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LTK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LTK FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=BEF:BERYLLIUM+TRIFLUORIDE+ION'>BEF</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.241Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=BEF:BERYLLIUM+TRIFLUORIDE+ION'>BEF</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=5ltk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ltk OCA], [https://pdbe.org/5ltk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ltk RCSB], [https://www.ebi.ac.uk/pdbsum/5ltk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ltk ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/G0RY84_CHATD G0RY84_CHATD] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 21: | Line 22: | ||
==See Also== | ==See Also== | ||
*[[Helicase 3D structures|Helicase 3D structures]] | *[[Helicase 3D structures|Helicase 3D structures]] | ||
*[[Pre-mRNA splicing factors 3D structures|Pre-mRNA splicing factors 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Chaetomium thermophilum var. thermophilum DSM 1495]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Ficner | [[Category: Ficner R]] | ||
[[Category: Tauchert | [[Category: Tauchert MJ]] | ||
Latest revision as of 21:48, 18 October 2023
Crystal structure of the Prp43-ADP-BeF3 complex (in hexagonal space group)Crystal structure of the Prp43-ADP-BeF3 complex (in hexagonal space group)
Structural highlights
FunctionPublication Abstract from PubMedThe DEAH-box helicase Prp43 is a key player in pre-mRNA splicing as well as the maturation of rRNAs. The exact modus operandi of Prp43 and of all other spliceosomal DEAH-box RNA helicases is still elusive. Here, we report crystal structures of Prp43 complexes in different functional states and the analysis of structure-based mutants providing insights into the unwinding and loading mechanism of RNAs. The Prp43*ATP-analog*RNA complex shows the localization of the RNA inside a tunnel formed by the two RecA-like and C-terminal domains. In the ATP-bound state this tunnel can be transformed into a groove prone for RNA binding by large rearrangements of the C-terminal domains. Several conformational changes between the ATP- and ADP-bound states explain the coupling of ATP hydrolysis to RNA translocation, mainly mediated by a beta-turn of the RecA1 domain containing the newly identified RF motif. This mechanism is clearly different to those of other RNA helicases. Structural insights into the mechanism of the DEAH-box RNA helicase Prp43.,Tauchert MJ, Fourmann JB, Luhrmann R, Ficner R Elife. 2017 Jan 16;6. pii: e21510. doi: 10.7554/eLife.21510. PMID:28092261[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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