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1m46

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[[Image:1m46.gif|left|200px]]
 
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{{Structure
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==CRYSTAL STRUCTURE OF MLC1P BOUND TO IQ4 OF MYO2P, A CLASS V MYOSIN==
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|PDB= 1m46 |SIZE=350|CAPTION= <scene name='initialview01'>1m46</scene>, resolution 2.103&Aring;
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<StructureSection load='1m46' size='340' side='right'caption='[[1m46]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1m46]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] and [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=1M46 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M46 FirstGlance]. <br>
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|ACTIVITY=
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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]] 2.103&#8491;</td></tr>
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|GENE= MLC1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
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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=1m46 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m46 OCA], [https://pdbe.org/1m46 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m46 RCSB], [https://www.ebi.ac.uk/pdbsum/1m46 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m46 ProSAT]</span></td></tr>
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}}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/MLC1_YEAST MLC1_YEAST] Essential light chain for the class II conventional myosin MYO1. Acts also as light chain for the class V unconventional myosin MYO2 and for IQG1. Involved in the assembly of the contractile actomyosin ring at the bud neck during cytokinesis by recruiting IQG1 to the bud neck. Also required for chitin and MYO2-dependent secretory vesicle deposition to the center of the bud neck for septum formation. May stabilize MYO2 by binding to its IQ domains. Its major function is probably not to regulate MYO1 activity, but rather to coordinate actin ring formation and targeted membrane deposition during cytokinesis via its interactions with MYO1, IQG1 and MYO2.<ref>PMID:9700160</ref> <ref>PMID:12456647</ref> <ref>PMID:15210731</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/m4/1m46_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</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/main_output.php?pdb_ID=1m46 ConSurf].
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<div style="clear:both"></div>
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'''CRYSTAL STRUCTURE OF MLC1P BOUND TO IQ4 OF MYO2P, A CLASS V MYOSIN'''
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==See Also==
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*[[Myosin 3D Structures|Myosin 3D Structures]]
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== References ==
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==Overview==
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<references/>
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IQ motifs are widespread in nature. Mlc1p is a calmodulin-like myosin light chain that binds to IQ motifs of a class V myosin, Myo2p, and an IQGAP-related protein, Iqg1p, playing a role in polarized growth and cytokinesis in Saccharomyces cerevisiae. The crystal structures of Mlc1p bound to IQ2 and IQ4 of Myo2p differ dramatically. When bound to IQ2, Mlc1p adopts a compact conformation in which both the N- and C-lobes interact with the IQ motif. However, in the complex with IQ4, the N-lobe no longer interacts with the IQ motif, resulting in an extended conformation of Mlc1p. The two light chain structures relate to two distinct subfamilies of IQ motifs, one of which does not interact with the N-lobes of calmodulin-like light chains. The correlation between light chain structure and IQ sequence is demonstrated further by sedimentation velocity analysis of complexes of Mlc1p with IQ motifs from Myo2p and Iqg1p. The resulting 'free' N-lobes of myosin light chains in the extended conformation could mediate the formation of ternary complexes during protein localization and/or partner recruitment.
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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1M46 is a [[Protein complex]] structure of sequences 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=1M46 OCA].
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==Reference==
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Two distinct myosin light chain structures are induced by specific variations within the bound IQ motifs-functional implications., Terrak M, Wu G, Stafford WF, Lu RC, Dominguez R, EMBO J. 2003 Feb 3;22(3):362-71. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12554638 12554638]
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[[Category: Protein complex]]
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Dominguez, R.]]
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[[Category: Saccharomyces cerevisiae S288C]]
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[[Category: Terrak, M.]]
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[[Category: Dominguez R]]
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[[Category: iq motif]]
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[[Category: Terrak M]]
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[[Category: myosin light chain]]
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[[Category: protein-peptide complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:38:39 2008''
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Current revision

CRYSTAL STRUCTURE OF MLC1P BOUND TO IQ4 OF MYO2P, A CLASS V MYOSIN

PDB ID 1m46

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