3mmi
From Proteopedia
(Difference between revisions)
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==Crystal structure of the globular tail of Myo4p== | ==Crystal structure of the globular tail of Myo4p== | ||
| - | <StructureSection load='3mmi' size='340' side='right' caption='[[3mmi]], [[Resolution|resolution]] 2.30Å' scene=''> | + | <StructureSection load='3mmi' size='340' side='right'caption='[[3mmi]], [[Resolution|resolution]] 2.30Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3mmi]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3mmi]] 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=3MMI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MMI FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3mmi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mmi OCA], [https://pdbe.org/3mmi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mmi RCSB], [https://www.ebi.ac.uk/pdbsum/3mmi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mmi ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/MYO4_YEAST MYO4_YEAST] Part of the mRNA localization machinery that restricts accumulation of certain proteins to the bud and in the daughter cell. Recruited to specific mRNAs including the ASH1 mRNA, coding for a repressor of the HO endonuclease, via its interaction with SHE3.<ref>PMID:10212145</ref> <ref>PMID:11032818</ref> <ref>PMID:11101531</ref> <ref>PMID:12499354</ref> <ref>PMID:15328357</ref> <ref>PMID:20439999</ref> |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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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=3mmi ConSurf]. | </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=3mmi ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Type V myosin (MyoV)-dependent transport of cargo is an essential process in eukaryotes. Studies on yeast and vertebrate MyoV showed that their globular tails mediate binding to the cargo complexes. In Saccharomyces cerevisiae, the MyoV motor Myo4p interacts with She3p to localize asymmetric synthesis of HO 1 (ASH1) mRNA into the bud of dividing cells. A recent study showed that localization of GFP-MS2-tethered ASH1 particles does not require the Myo4p globular tail, challenging the supposed role of this domain. We assessed ASH1 mRNA and Myo4p distribution more directly and found that their localization is impaired in cells expressing globular tail-lacking Myo4p. In vitro studies further show that the globular tail together with a more N-terminal linker region is required for efficient She3p binding. We also determined the x-ray structure of the Myo4p globular tail and identify a conserved surface patch important for She3p binding. The structure shows pronounced similarities to membrane-tethering complexes and indicates that Myo4p may not undergo auto-inhibition of its motor domain. | ||
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| - | The structure of the Myo4p globular tail and its function in ASH1 mRNA localization.,Heuck A, Fetka I, Brewer DN, Huls D, Munson M, Jansen RP, Niessing D J Cell Biol. 2010 May 3;189(3):497-510. PMID:20439999<ref>PMID:20439999</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 3mmi" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
| - | *[[Myosin|Myosin]] | + | *[[Myosin 3D Structures|Myosin 3D Structures]] |
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: | + | [[Category: Heuck A]] |
| - | [[Category: | + | [[Category: Niessing D]] |
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Current revision
Crystal structure of the globular tail of Myo4p
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