|
|
| (One intermediate revision not shown.) |
| Line 1: |
Line 1: |
| | | | |
| | ==Solution Structure of the Prp40 WW Domain Pair of the Yeast Splicing Factor Prp40== | | ==Solution Structure of the Prp40 WW Domain Pair of the Yeast Splicing Factor Prp40== |
| - | <StructureSection load='1o6w' size='340' side='right'caption='[[1o6w]], [[NMR_Ensembles_of_Models | 7 NMR models]]' scene=''> | + | <StructureSection load='1o6w' size='340' side='right'caption='[[1o6w]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1o6w]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O6W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1O6W FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1o6w]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O6W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1O6W FirstGlance]. <br> |
| - | </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=1o6w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o6w OCA], [https://pdbe.org/1o6w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1o6w RCSB], [https://www.ebi.ac.uk/pdbsum/1o6w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1o6w ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1o6w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o6w OCA], [https://pdbe.org/1o6w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1o6w RCSB], [https://www.ebi.ac.uk/pdbsum/1o6w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1o6w ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/PRP40_YEAST PRP40_YEAST]] Required for pre-spliceosome formation, which is the first step of pre-mRNA splicing. This protein is associated with snRNP U1. Two commitment complexes, CC1 and CC2, have been defined in yeast. CC1 is a basal complex dependent only on the 5' splice site. CC2 is a complex of lower mobility and is dependent on a branchpoint as well as a 5' splice site region. This protein is involved in CC2 formation where it binds to the branchpoint binding protein MSL5, bridging the U1 snRNP-associated 5' splice site and the MSL5-associated branch point 3' intron splice site.<ref>PMID:9150140</ref> <ref>PMID:10978320</ref> <ref>PMID:15020406</ref>
| + | [https://www.uniprot.org/uniprot/PRP40_YEAST PRP40_YEAST] Required for pre-spliceosome formation, which is the first step of pre-mRNA splicing. This protein is associated with snRNP U1. Two commitment complexes, CC1 and CC2, have been defined in yeast. CC1 is a basal complex dependent only on the 5' splice site. CC2 is a complex of lower mobility and is dependent on a branchpoint as well as a 5' splice site region. This protein is involved in CC2 formation where it binds to the branchpoint binding protein MSL5, bridging the U1 snRNP-associated 5' splice site and the MSL5-associated branch point 3' intron splice site.<ref>PMID:9150140</ref> <ref>PMID:10978320</ref> <ref>PMID:15020406</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 34: |
Line 35: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 18824]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Macias, M J]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Sattler, M]] | + | [[Category: Macias MJ]] |
| - | [[Category: Stier, G]] | + | [[Category: Sattler M]] |
| - | [[Category: Wiesner, S]] | + | [[Category: Stier G]] |
| - | [[Category: Mrna processing]]
| + | [[Category: Wiesner S]] |
| - | [[Category: Mrna splicing]]
| + | |
| - | [[Category: Nuclear protein]]
| + | |
| - | [[Category: Prp40]]
| + | |
| - | [[Category: Ribonucleoprotein]]
| + | |
| - | [[Category: Ww domain pair]]
| + | |
| Structural highlights
Function
PRP40_YEAST Required for pre-spliceosome formation, which is the first step of pre-mRNA splicing. This protein is associated with snRNP U1. Two commitment complexes, CC1 and CC2, have been defined in yeast. CC1 is a basal complex dependent only on the 5' splice site. CC2 is a complex of lower mobility and is dependent on a branchpoint as well as a 5' splice site region. This protein is involved in CC2 formation where it binds to the branchpoint binding protein MSL5, bridging the U1 snRNP-associated 5' splice site and the MSL5-associated branch point 3' intron splice site.[1] [2] [3]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The yeast splicing factor pre-mRNA processing protein 40 (Prp40) comprises two N-terminal WW domains, separated by a ten-residue linker, and six consecutive FF domains. In the spliceosome, the Prp40 WW domains participate in cross-intron bridging by interacting with proline-rich regions present in the branch-point binding protein (BBP) and the U5 small nuclear ribonucleoprotein component Prp8. Furthermore, binding of Prp40 to the phosphorylated C-terminal domain (CTD) of the largest subunit of RNA polymerase II is thought to link splicing to transcription. To gain insight into this complex interaction network we have determined the solution structure of the tandem Prp40 WW domains by NMR spectroscopy and performed chemical shift mapping experiments with different proline-rich peptides. The WW domains each adopt the characteristic triple-stranded beta-sheet structure and are connected by a stable alpha-helical linker. On the basis of a detailed analysis of residual dipolar couplings (RDC) and 15N relaxation data we show that the tandem Prp40 WW domains behave in solution as a single folded unit with unique alignment and diffusion tensor, respectively. Using [1H-15N]-RDCs, we were able to accurately define the relative orientation of the WW domains revealing that the binding pockets of each domain face opposite sides of the structure. Furthermore, we found that both Prp40 WW domains interact with PPxY motifs (where x is any residue) present in peptides derived from the splicing factors BBP and Prp8. Moreover, the Prp40 WW domains are shown to bind proline-rich peptides devoid of aromatic residues, which are also recognised by the Abl-SH3 domain and the WW domain of the mammalian Prp40 orthologue formin binding protein 11. In contrast, no interaction was observed between the Prp40 WW domains and the CTD repeats used in this work.
Solution structure and ligand recognition of the WW domain pair of the yeast splicing factor Prp40.,Wiesner S, Stier G, Sattler M, Macias MJ J Mol Biol. 2002 Dec 6;324(4):807-22. PMID:12460579[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Abovich N, Rosbash M. Cross-intron bridging interactions in the yeast commitment complex are conserved in mammals. Cell. 1997 May 2;89(3):403-12. PMID:9150140
- ↑ Morris DP, Greenleaf AL. The splicing factor, Prp40, binds the phosphorylated carboxyl-terminal domain of RNA polymerase II. J Biol Chem. 2000 Dec 22;275(51):39935-43. PMID:10978320 doi:10.1074/jbc.M004118200
- ↑ Murphy MW, Olson BL, Siliciano PG. The yeast splicing factor Prp40p contains functional leucine-rich nuclear export signals that are essential for splicing. Genetics. 2004 Jan;166(1):53-65. PMID:15020406
- ↑ Wiesner S, Stier G, Sattler M, Macias MJ. Solution structure and ligand recognition of the WW domain pair of the yeast splicing factor Prp40. J Mol Biol. 2002 Dec 6;324(4):807-22. PMID:12460579
|
