6bk8

From Proteopedia

(Difference between revisions)

Current revision

S. cerevisiae spliceosomal post-catalytic P complex

6bk8, resolution 3.30Å

Structural highlights

6bk8 is a 13 chain structure with sequence from Saccharomyces cerevisiae S288C. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 3.3Å
Ligands:
Experimental data:	Check to display Experimental Data
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SLT11_YEAST Involved in pre-mRNA splicing. Facilitates the cooperative formation of U2/U6 helix II in association with stem II in the spliceosome. Binds to RNA.^[1] ^[2]

Publication Abstract from PubMed

The spliceosome undergoes dramatic changes in a splicing cycle. Structures of B, B(act), C, C*, and intron lariat spliceosome complexes revealed mechanisms of 5'-splice site (ss) recognition, branching, and intron release, but lacked information on 3'-ss recognition, exon ligation, and exon release. Here we report a cryo-electron microscopy structure of the postcatalytic P complex at 3.3-angstrom resolution, revealing that the 3' ss is mainly recognized through non-Watson-Crick base pairing with the 5' ss and branch point. Furthermore, one or more unidentified proteins become stably associated with the P complex, securing the 3' exon and potentially regulating activity of the helicase Prp22. Prp22 binds nucleotides 15 to 21 in the 3' exon, enabling it to pull the intron-exon or ligated exons in a 3' to 5' direction to achieve 3'-ss proofreading or exon release, respectively.

Structure of the yeast spliceosomal postcatalytic P complex.,Liu S, Li X, Zhang L, Jiang J, Hill RC, Cui Y, Hansen KC, Zhou ZH, Zhao R Science. 2017 Dec 8;358(6368):1278-1283. doi: 10.1126/science.aar3462. Epub 2017 , Nov 16. PMID:29146870^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Xu D, Friesen JD. Splicing factor slt11p and its involvement in formation of U2/U6 helix II in activation of the yeast spliceosome. Mol Cell Biol. 2001 Feb;21(4):1011-23. PMID:11158289 doi:http://dx.doi.org/10.1128/MCB.21.4.1011-1023.2001
↑ Xu D, Field DJ, Tang SJ, Moris A, Bobechko BP, Friesen JD. Synthetic lethality of yeast slt mutations with U2 small nuclear RNA mutations suggests functional interactions between U2 and U5 snRNPs that are important for both steps of pre-mRNA splicing. Mol Cell Biol. 1998 Apr;18(4):2055-66. PMID:9528778
↑ Liu S, Li X, Zhang L, Jiang J, Hill RC, Cui Y, Hansen KC, Zhou ZH, Zhao R. Structure of the yeast spliceosomal postcatalytic P complex. Science. 2017 Dec 8;358(6368):1278-1283. doi: 10.1126/science.aar3462. Epub 2017 , Nov 16. PMID:29146870 doi:http://dx.doi.org/10.1126/science.aar3462

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6bk8"

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 6bk8 is ON HOLD
+==S. cerevisiae spliceosomal post-catalytic P complex==
+<SX load='6bk8' size='340' side='right' viewer='molstar' caption='[[6bk8]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6bk8]] is a 13 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=6BK8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6BK8 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.3&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=IHP:INOSITOL+HEXAKISPHOSPHATE'>IHP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=6bk8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bk8 OCA], [https://pdbe.org/6bk8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6bk8 RCSB], [https://www.ebi.ac.uk/pdbsum/6bk8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6bk8 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/SLT11_YEAST SLT11_YEAST] Involved in pre-mRNA splicing. Facilitates the cooperative formation of U2/U6 helix II in association with stem II in the spliceosome. Binds to RNA.<ref>PMID:11158289</ref> <ref>PMID:9528778</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The spliceosome undergoes dramatic changes in a splicing cycle. Structures of B, B(act), C, C*, and intron lariat spliceosome complexes revealed mechanisms of 5'-splice site (ss) recognition, branching, and intron release, but lacked information on 3'-ss recognition, exon ligation, and exon release. Here we report a cryo-electron microscopy structure of the postcatalytic P complex at 3.3-angstrom resolution, revealing that the 3' ss is mainly recognized through non-Watson-Crick base pairing with the 5' ss and branch point. Furthermore, one or more unidentified proteins become stably associated with the P complex, securing the 3' exon and potentially regulating activity of the helicase Prp22. Prp22 binds nucleotides 15 to 21 in the 3' exon, enabling it to pull the intron-exon or ligated exons in a 3' to 5' direction to achieve 3'-ss proofreading or exon release, respectively.
-Authors:
+Structure of the yeast spliceosomal postcatalytic P complex.,Liu S, Li X, Zhang L, Jiang J, Hill RC, Cui Y, Hansen KC, Zhou ZH, Zhao R Science. 2017 Dec 8;358(6368):1278-1283. doi: 10.1126/science.aar3462. Epub 2017 , Nov 16. PMID:29146870<ref>PMID:29146870</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 6bk8" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Nucleoprotein 3D structures|Nucleoprotein 3D structures]]
+*[[Pre-mRNA splicing factors 3D structures|Pre-mRNA splicing factors 3D structures]]
+*[[Sm-like protein 3D structures|Sm-like protein 3D structures]]
+== References ==
+<references/>
+__TOC__
+</SX>
+[[Category: Large Structures]]
+[[Category: Saccharomyces cerevisiae S288C]]
+[[Category: Li X]]
+[[Category: Liu S]]
+[[Category: Zhao R]]
+[[Category: Zhou ZH]]

6bk8

From Proteopedia

Current revision

S. cerevisiae spliceosomal post-catalytic P complex

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

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