1zuy

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==High-resolution structure of yeast Myo5 SH3 domain==
==High-resolution structure of yeast Myo5 SH3 domain==
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<StructureSection load='1zuy' size='340' side='right' caption='[[1zuy]], [[Resolution|resolution]] 1.39&Aring;' scene=''>
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<StructureSection load='1zuy' size='340' side='right'caption='[[1zuy]], [[Resolution|resolution]] 1.39&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1zuy]] is a 2 chain structure 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=1ZUY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ZUY FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1zuy]] is a 2 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=1ZUY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZUY FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.39&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1yp5|1yp5]]</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=IPA:ISOPROPYL+ALCOHOL'>IPA</scene></td></tr>
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<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=1zuy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zuy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1zuy RCSB], [http://www.ebi.ac.uk/pdbsum/1zuy PDBsum]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1zuy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zuy OCA], [https://pdbe.org/1zuy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zuy RCSB], [https://www.ebi.ac.uk/pdbsum/1zuy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zuy ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/MYO5_YEAST MYO5_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:9628892</ref> <ref>PMID:10944111</ref> <ref>PMID:10648568</ref> <ref>PMID:10648569</ref> <ref>PMID:12725728</ref> <ref>PMID:12808026</ref> <ref>PMID:16478726</ref>
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[https://www.uniprot.org/uniprot/MYO5_YEAST MYO5_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:9628892</ref> <ref>PMID:10944111</ref> <ref>PMID:10648568</ref> <ref>PMID:10648569</ref> <ref>PMID:12725728</ref> <ref>PMID:12808026</ref> <ref>PMID:16478726</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zu/1zuy_consurf.spt"</scriptWhenChecked>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zu/1zuy_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmolCheckbox>
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</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/chain_selection.php?pdb_ID=2ata ConSurf].
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</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=1zuy ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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==See Also==
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*[[Myosin 3D Structures|Myosin 3D Structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Cesareni, G]]
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[[Category: Cesareni G]]
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[[Category: Ferracuti, S]]
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[[Category: Ferracuti S]]
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[[Category: Gonfloni, S]]
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[[Category: Gonfloni S]]
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[[Category: Kursula, P]]
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[[Category: Kursula P]]
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[[Category: Wilmanns, M]]
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[[Category: Wilmanns M]]
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[[Category: Contractile protein]]
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[[Category: Sh3 domain]]
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Current revision

High-resolution structure of yeast Myo5 SH3 domain

PDB ID 1zuy

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