1va7: Difference between revisions

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[[Image:1va7.png|left|200px]]


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==Yeast Myo3 SH3 domain, triclinic crystal form==
The line below this paragraph, containing "STRUCTURE_1va7", creates the "Structure Box" on the page.
<StructureSection load='1va7' size='340' side='right'caption='[[1va7]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1va7]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VA7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VA7 FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
{{STRUCTURE_1va7|  PDB=1va7  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1va7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1va7 OCA], [https://pdbe.org/1va7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1va7 RCSB], [https://www.ebi.ac.uk/pdbsum/1va7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1va7 ProSAT]</span></td></tr>
 
</table>
===Yeast Myo3 SH3 domain, triclinic crystal form===
== Function ==
 
[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 ==
==About this Structure==
[[Image:Consurf_key_small.gif|200px|right]]
[[1va7]] is a 4 chain structure of [[Myosin]] with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VA7 OCA].  
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/va/1va7_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1va7 ConSurf].
<div style="clear:both"></div>


==See Also==
==See Also==
*[[Myosin]]
*[[Myosin 3D Structures|Myosin 3D Structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Kursula, P.]]
[[Category: Kursula P]]
[[Category: Lehmann, F.]]
[[Category: Lehmann F]]
[[Category: Song, Y H.]]
[[Category: Song YH]]
[[Category: Wilmanns, M.]]
[[Category: Wilmanns M]]
[[Category: Contractile protein]]
[[Category: Sh3 domain]]
[[Category: Structural genomic]]

Latest revision as of 10:50, 25 October 2023

Yeast Myo3 SH3 domain, triclinic crystal formYeast Myo3 SH3 domain, triclinic crystal form

Structural highlights

1va7 is a 4 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.9Å
Ligands:
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.

See Also

References

  1. ↑ 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
  2. ↑ 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
  3. ↑ 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
  4. ↑ 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
  5. ↑ 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
  6. ↑ 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
  7. ↑ 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

1va7, resolution 2.90Å

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