2btt

From Proteopedia

(Difference between revisions)

Revision as of 13:39, 13 October 2021

NMR Structure of MYO3-SH3 domain from Myosin-typeI from S. cerevisiae

Structural highlights

2btt is a 1 chain structure with sequence from Atcc 18824. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1ruw
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[MYO3_YEAST] One of two redundant type-I myosins implicated in the organization of the actin cytoskeleton. Required for proper actin cytoskeleton polarization and for the internalization step in endocytosis. At the cell cortex, assembles in patch-like structures together with proteins from the actin-polymerizing machinery and promotes actin assembly. Functions redundantly with LAS17 as actin nucleation-promoting factor (NPF) for the Arp2/3 complex. Motor domain phosphorylation by PAK kinases CLA4 and STE20 promotes CDC42-regulated actin assembly. Functions together with the NPF PAN1 in late stages of endocytosis. Motor domain phosphorylation by PDK1 kinases PKH1 and PKH2, and by SGK kinases YPK1 and YPK2, promotes ligand-induced, but not constitutive endocytosis of the G protein-coupled receptor STE2.^[1] ^[2] ^[3] ^[4] ^[5] ^[6] ^[7]

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

SH3 domains are small protein modules that are involved in protein-protein interactions in several essential metabolic pathways. The availability of the complete genome and the limited number of clearly identifiable SH3 domains make the yeast Saccharomyces cerevisae an ideal proteomic-based model system to investigate the structural rules dictating the SH3-mediated protein interactions and to develop new tools to assist these studies. In the present work, we have determined the solution structure of the SH3 domain from Myo3 and modeled by homology that of the highly homologous Myo5, two myosins implicated in actin polymerization. We have then implemented an integrated approach that makes use of experimental and computational methods to characterize their binding properties. While accommodating their targets in the classical groove, the two domains have selectivity in both orientation and sequence specificity of the target peptides. From our study, we propose a consensus sequence that may provide a useful guideline to identify new natural partners and suggest a strategy of more general applicability that may be of use in other structural proteomic studies.

New approaches to high-throughput structure characterization of SH3 complexes: the example of Myosin-3 and Myosin-5 SH3 domains from S. cerevisiae.,Musi V, Birdsall B, Fernandez-Ballester G, Guerrini R, Salvatori S, Serrano L, Pastore A Protein Sci. 2006 Apr;15(4):795-807. PMID:16600966^[8]

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

References

↑ Goodson HV, Anderson BL, Warrick HM, Pon LA, Spudich JA. Synthetic lethality screen identifies a novel yeast myosin I gene (MYO5): myosin I proteins are required for polarization of the actin cytoskeleton. J Cell Biol. 1996 Jun;133(6):1277-91. PMID:8682864
↑ Geli MI, Riezman H. Role of type I myosins in receptor-mediated endocytosis in yeast. Science. 1996 Apr 26;272(5261):533-5. PMID:8614799
↑ Wu C, Lytvyn V, Thomas DY, Leberer E. The phosphorylation site for Ste20p-like protein kinases is essential for the function of myosin-I in yeast. J Biol Chem. 1997 Dec 5;272(49):30623-6. PMID:9388196
↑ Evangelista M, Klebl BM, Tong AH, Webb BA, Leeuw T, Leberer E, Whiteway M, Thomas DY, Boone C. A role for myosin-I in actin assembly through interactions with Vrp1p, Bee1p, and the Arp2/3 complex. J Cell Biol. 2000 Jan 24;148(2):353-62. PMID:10648568
↑ Lechler T, Shevchenko A, Li R. Direct involvement of yeast type I myosins in Cdc42-dependent actin polymerization. J Cell Biol. 2000 Jan 24;148(2):363-73. PMID:10648569
↑ Wesche S, Arnold M, Jansen RP. The UCS domain protein She4p binds to myosin motor domains and is essential for class I and class V myosin function. Curr Biol. 2003 Apr 29;13(9):715-24. PMID:12725728
↑ Toi H, Fujimura-Kamada K, Irie K, Takai Y, Todo S, Tanaka K. She4p/Dim1p interacts with the motor domain of unconventional myosins in the budding yeast, Saccharomyces cerevisiae. Mol Biol Cell. 2003 Jun;14(6):2237-49. Epub 2003 Feb 6. PMID:12808026 doi:http://dx.doi.org/10.1091/mbc.E02-09-0616
↑ Musi V, Birdsall B, Fernandez-Ballester G, Guerrini R, Salvatori S, Serrano L, Pastore A. New approaches to high-throughput structure characterization of SH3 complexes: the example of Myosin-3 and Myosin-5 SH3 domains from S. cerevisiae. Protein Sci. 2006 Apr;15(4):795-807. PMID:16600966 doi:15/4/795

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2btt"

@@ Line 3: / Line 3: @@
 <StructureSection load='2btt' size='340' side='right'caption='[[2btt]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2btt]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BTT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BTT FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2btt]] 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=2BTT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BTT FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ruw|1ruw]]</td></tr>
+</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ruw|1ruw]]</div></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2btt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2btt OCA], [http://pdbe.org/2btt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2btt RCSB], [http://www.ebi.ac.uk/pdbsum/2btt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2btt 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=2btt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2btt OCA], [https://pdbe.org/2btt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2btt RCSB], [https://www.ebi.ac.uk/pdbsum/2btt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2btt ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/MYO3_YEAST MYO3_YEAST]] One of two redundant type-I myosins implicated in the organization of the actin cytoskeleton. Required for proper actin cytoskeleton polarization and for the internalization step in endocytosis. At the cell cortex, assembles in patch-like structures together with proteins from the actin-polymerizing machinery and promotes actin assembly. Functions redundantly with LAS17 as actin nucleation-promoting factor (NPF) for the Arp2/3 complex. Motor domain phosphorylation by PAK kinases CLA4 and STE20 promotes CDC42-regulated actin assembly. Functions together with the NPF PAN1 in late stages of endocytosis. Motor domain phosphorylation by PDK1 kinases PKH1 and PKH2, and by SGK kinases YPK1 and YPK2, promotes ligand-induced, but not constitutive endocytosis of the G protein-coupled receptor STE2.<ref>PMID:8682864</ref> <ref>PMID:8614799</ref> <ref>PMID:9388196</ref> <ref>PMID:10648568</ref> <ref>PMID:10648569</ref> <ref>PMID:12725728</ref> <ref>PMID:12808026</ref>
+[[https://www.uniprot.org/uniprot/MYO3_YEAST MYO3_YEAST]] One of two redundant type-I myosins implicated in the organization of the actin cytoskeleton. Required for proper actin cytoskeleton polarization and for the internalization step in endocytosis. At the cell cortex, assembles in patch-like structures together with proteins from the actin-polymerizing machinery and promotes actin assembly. Functions redundantly with LAS17 as actin nucleation-promoting factor (NPF) for the Arp2/3 complex. Motor domain phosphorylation by PAK kinases CLA4 and STE20 promotes CDC42-regulated actin assembly. Functions together with the NPF PAN1 in late stages of endocytosis. Motor domain phosphorylation by PDK1 kinases PKH1 and PKH2, and by SGK kinases YPK1 and YPK2, promotes ligand-induced, but not constitutive endocytosis of the G protein-coupled receptor STE2.<ref>PMID:8682864</ref> <ref>PMID:8614799</ref> <ref>PMID:9388196</ref> <ref>PMID:10648568</ref> <ref>PMID:10648569</ref> <ref>PMID:12725728</ref> <ref>PMID:12808026</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

2btt

From Proteopedia

Revision as of 13:39, 13 October 2021

NMR Structure of MYO3-SH3 domain from Myosin-typeI from S. cerevisiae

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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