4pj3: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4pj3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PJ3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PJ3 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4pj3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PJ3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PJ3 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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]] 2.3Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=4pj3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pj3 OCA], [https://pdbe.org/4pj3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pj3 RCSB], [https://www.ebi.ac.uk/pdbsum/4pj3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pj3 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=4pj3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pj3 OCA], [https://pdbe.org/4pj3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pj3 RCSB], [https://www.ebi.ac.uk/pdbsum/4pj3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pj3 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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</div> | </div> | ||
<div class="pdbe-citations 4pj3" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 4pj3" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Helicase 3D structures|Helicase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> |
Latest revision as of 03:44, 28 December 2023
Structural insight into the function and evolution of the spliceosomal helicase Aquarius, Structure of Aquarius in complex with AMPPNPStructural insight into the function and evolution of the spliceosomal helicase Aquarius, Structure of Aquarius in complex with AMPPNP
Structural highlights
FunctionAQR_HUMAN Intron-binding spliceosomal protein required to link pre-mRNA splicing and snoRNP (small nucleolar ribonucleoprotein) biogenesis. Plays a key role in position-dependent assembly of intron-encoded box C/D small snoRNP, splicing being required for snoRNP assembly. May act by helping the folding of the snoRNA sequence. Binds to intron of pre-mRNAs in a sequence-independent manner, contacting the region between snoRNA and the branchpoint of introns (40 nucleotides upstream of the branchpoint) during the late stages of splicing.[1] Publication Abstract from PubMedAquarius is a multifunctional putative RNA helicase that binds precursor-mRNA introns at a defined position. Here we report the crystal structure of human Aquarius, revealing a central RNA helicase core and several unique accessory domains, including an ARM-repeat domain. We show that Aquarius is integrated into spliceosomes as part of a pentameric intron-binding complex (IBC) that, together with the ARM domain, cross-links to U2 snRNP proteins within activated spliceosomes; this suggests that the latter aid in positioning Aquarius on the intron. Aquarius's ARM domain is essential for IBC formation, thus indicating that it has a key protein-protein-scaffolding role. Finally, we provide evidence that Aquarius is required for efficient precursor-mRNA splicing in vitro. Our findings highlight the remarkable structural adaptations of a helicase to achieve position-specific recruitment to a ribonucleoprotein complex and reveal a new building block of the human spliceosome. The RNA helicase Aquarius exhibits structural adaptations mediating its recruitment to spliceosomes.,De I, Bessonov S, Hofele R, Dos Santos K, Will CL, Urlaub H, Luhrmann R, Pena V Nat Struct Mol Biol. 2015 Feb;22(2):138-44. doi: 10.1038/nsmb.2951. Epub 2015 Jan, 19. PMID:25599396[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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