4ll6: Difference between revisions

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==Structure of Myo4p globular tail domain.==
==Structure of Myo4p globular tail domain.==
<StructureSection load='4ll6' size='340' side='right' caption='[[4ll6]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='4ll6' size='340' side='right'caption='[[4ll6]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4ll6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LL6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LL6 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4ll6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LL6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LL6 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ll7|4ll7]], [[4ll8|4ll8]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MYO4, SHE1, YAL029C, FUN22 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</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=4ll6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ll6 OCA], [https://pdbe.org/4ll6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ll6 RCSB], [https://www.ebi.ac.uk/pdbsum/4ll6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ll6 ProSAT]</span></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=4ll6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ll6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ll6 RCSB], [http://www.ebi.ac.uk/pdbsum/4ll6 PDBsum]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://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> 
[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>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Myosin 4 protein (Myo4p), one of five distinct myosins of yeast, is dedicated to cytoplasmic transport of two types of cargos, zipcoded messenger ribonucleoprotein particles (mRNPs) and tubular endoplasmic reticulum (tER). Neither cargo binds directly to Myo4p. Instead, swi5p-dependent HO expression 3 protein (She3p) serves as an "adaptor" that contains three binding modules, one for Myo4p and one each for zipcoded mRNP and tER. The assembly of a transport-competent motor complex is poorly understood. Here, we report that Myo4p*She3p forms a stable 1:2 heterotrimer in solution. In the Myo4p*She3p crystal structure, Myo4p's C-terminal domain (CTD) assumes a lobster claw-shaped form, the minor prong of which adheres to a pseudocoiled-coil region of She3p. The extensive Myo4p*She3p interactome buries 3,812 A(2) surface area and is primarily hydrophobic. Because the Myo4p*She3p heterotrimer contains only one myosin molecule, it is not transport-competent. By stepwise reconstitution, we found a single molecule of synthetic oligonucleotide (representing the mRNA zipcode element) bound to a single tetramer of zipcode binding protein She2p to be sufficient for Myo4p*She3p dimerization. Therefore, cargo initiates cross-linking of two Myo4p*She3p heterotrimers to an ensemble that contains two myosin molecules obligatory for movement. An additional crystal structure comprising an overlapping upstream portion of She3p showed continuation of the pseudocoiled-coil structure and revealed another highly conserved surface region. We suggest this region as a candidate binding site for a yet unidentified tER ligand. We propose a model whereby zipcoded mRNP and/or tER ligands couple two Myo4p*She3p heterotrimers and thereby generate a transport-competent motor complex either for separate transport or cotransport of these two cargos.
 
Structure of a myosin*adaptor complex and pairing by cargo.,Shi H, Singh N, Esselborn F, Blobel G Proc Natl Acad Sci U S A. 2014 Mar 25;111(12):E1082-90. doi:, 10.1073/pnas.1401428111. Epub 2014 Feb 12. PMID:24522109<ref>PMID:24522109</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>


==See Also==
==See Also==
*[[Myosin|Myosin]]
*[[Myosin 3D Structures|Myosin 3D Structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Baker's yeast]]
[[Category: Large Structures]]
[[Category: Blobel, G]]
[[Category: Saccharomyces cerevisiae S288C]]
[[Category: Esselborn, F]]
[[Category: Blobel G]]
[[Category: Shi, H]]
[[Category: Esselborn F]]
[[Category: Singh, N]]
[[Category: Shi H]]
[[Category: Globular tail domain]]
[[Category: Singh N]]
[[Category: Motor protein]]
[[Category: Mrna localization]]
[[Category: Myo4p]]

Latest revision as of 15:20, 1 March 2024

Structure of Myo4p globular tail domain.Structure of Myo4p globular tail domain.

Structural highlights

4ll6 is a 1 chain structure with sequence from Saccharomyces cerevisiae S288C. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.3Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.[1] [2] [3] [4] [5] [6]

See Also

References

  1. ↑ Munchow S, Sauter C, Jansen RP. Association of the class V myosin Myo4p with a localised messenger RNA in budding yeast depends on She proteins. J Cell Sci. 1999 May;112 ( Pt 10):1511-8. PMID:10212145
  2. ↑ Bohl F, Kruse C, Frank A, Ferring D, Jansen RP. She2p, a novel RNA-binding protein tethers ASH1 mRNA to the Myo4p myosin motor via She3p. EMBO J. 2000 Oct 16;19(20):5514-24. PMID:11032818 doi:http://dx.doi.org/10.1093/emboj/19.20.5514
  3. ↑ Long RM, Gu W, Lorimer E, Singer RH, Chartrand P. She2p is a novel RNA-binding protein that recruits the Myo4p-She3p complex to ASH1 mRNA. EMBO J. 2000 Dec 1;19(23):6592-601. PMID:11101531 doi:http://dx.doi.org/10.1093/emboj/19.23.6592
  4. ↑ Kruse C, Jaedicke A, Beaudouin J, Bohl F, Ferring D, Guttler T, Ellenberg J, Jansen RP. Ribonucleoprotein-dependent localization of the yeast class V myosin Myo4p. J Cell Biol. 2002 Dec 23;159(6):971-82. Epub 2002 Dec 23. PMID:12499354 doi:http://dx.doi.org/10.1083/jcb.200207101
  5. ↑ Gonsalvez GB, Little JL, Long RM. ASH1 mRNA anchoring requires reorganization of the Myo4p-She3p-She2p transport complex. J Biol Chem. 2004 Oct 29;279(44):46286-94. Epub 2004 Aug 23. PMID:15328357 doi:http://dx.doi.org/10.1074/jbc.M406086200
  6. ↑ Heuck A, Fetka I, Brewer DN, Huls D, Munson M, Jansen RP, Niessing D. The structure of the Myo4p globular tail and its function in ASH1 mRNA localization. J Cell Biol. 2010 May 3;189(3):497-510. PMID:20439999 doi:10.1083/jcb.201002076

4ll6, resolution 2.30Å

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