1m45: Difference between revisions

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<StructureSection load='1m45' size='340' side='right'caption='[[1m45]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
<StructureSection load='1m45' size='340' side='right'caption='[[1m45]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1m45]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M45 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1M45 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1m45]] 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=1M45 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M45 FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1m46|1m46]]</div></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]] 1.65&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MLC1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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=1m45 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m45 OCA], [https://pdbe.org/1m45 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m45 RCSB], [https://www.ebi.ac.uk/pdbsum/1m45 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m45 ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1m45 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m45 OCA], [http://pdbe.org/1m45 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1m45 RCSB], [http://www.ebi.ac.uk/pdbsum/1m45 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1m45 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://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> [[http://www.uniprot.org/uniprot/MYO2_YEAST MYO2_YEAST]] Myosin heavy chain that is required for the cell cycle-regulated transport of various organelles and proteins for their segregation. Functions by binding with its tail domain to receptor proteins on organelles and exerting force with its N-terminal motor domain against actin filaments, thereby transporting its cargo along polarized actin cables. Essential for the delivery of secretory vesicles to sites of active growth during bud emergence and cytokinesis. Required for segregation and inheritance of peroxisomes, late Golgi compartments, mitochondria and the vacuole to the daughter cell during cell division. Also required for correct alignment of the spindle during mitosis.<ref>PMID:10931864</ref> <ref>PMID:11285273</ref> <ref>PMID:11381095</ref> <ref>PMID:11733545</ref> <ref>PMID:11781333</ref> <ref>PMID:12391144</ref> <ref>PMID:12743102</ref> <ref>PMID:21248204</ref> 
[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>  
== 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=1m45 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=1m45 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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:12554638<ref>PMID:12554638</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1m45" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 18824]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Dominguez, R]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Terrak, M]]
[[Category: Saccharomyces cerevisiae S288C]]
[[Category: Cell cycle protein]]
[[Category: Dominguez R]]
[[Category: Iq motif]]
[[Category: Terrak M]]
[[Category: Myosin light chain]]
[[Category: Protein-peptide complex]]

Latest revision as of 10:39, 14 February 2024

CRYSTAL STRUCTURE OF MLC1P BOUND TO IQ2 OF MYO2P, A CLASS V MYOSINCRYSTAL STRUCTURE OF MLC1P BOUND TO IQ2 OF MYO2P, A CLASS V MYOSIN

Structural highlights

1m45 is a 2 chain structure with sequence from Saccharomyces cerevisiae and 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 1.65Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.[1] [2] [3]

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. ↑ Stevens RC, Davis TN. Mlc1p is a light chain for the unconventional myosin Myo2p in Saccharomyces cerevisiae. J Cell Biol. 1998 Aug 10;142(3):711-22. PMID:9700160
  2. ↑ Wagner W, Bielli P, Wacha S, Ragnini-Wilson A. Mlc1p promotes septum closure during cytokinesis via the IQ motifs of the vesicle motor Myo2p. EMBO J. 2002 Dec 2;21(23):6397-408. PMID:12456647
  3. ↑ Luo J, Vallen EA, Dravis C, Tcheperegine SE, Drees B, Bi E. Identification and functional analysis of the essential and regulatory light chains of the only type II myosin Myo1p in Saccharomyces cerevisiae. J Cell Biol. 2004 Jun 21;165(6):843-55. PMID:15210731 doi:http://dx.doi.org/10.1083/jcb.200401040

1m45, resolution 1.65Å

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