1n2d - Revision history

OCA at 07:51, 14 February 2024

OCA — Wed, 14 Feb 2024 07:51:34 GMT

←Older revision		Revision as of 07:51, 14 February 2024
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	<StructureSection load='1n2d' size='340' side='right'caption='[[1n2d]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='1n2d' size='340' side='right'caption='[[1n2d]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1n2d]] is a 3 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=1N2D OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=1N2D FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1n2d]] is a 3 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=1N2D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1N2D 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;'>[[1m45\|1m45]], [[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]] 2Å</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=1n2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n2d OCA], [https://pdbe.org/1n2d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1n2d RCSB], [https://www.ebi.ac.uk/pdbsum/1n2d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1n2d 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=1n2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n2d OCA], [~~http~~://pdbe.org/1n2d PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1n2d RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1n2d PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1n2d 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=1n2d 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=1n2d ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Myosin V is a double-headed molecular motor involved in organelle transport. Two distinctive features of this motor, processivity and the ability to take extended linear steps of approximately 36 nm along the actin helical track, depend on its unusually long light chain-binding domain (LCBD). The LCBD of myosin V consists of six tandem IQ motifs, which constitute the binding sites for calmodulin (CaM) and CaM-like light chains. Here, we report the 2-A resolution crystal structure of myosin light chain 1 (Mlc1p) bound to the IQ2-IQ3 fragment of Myo2p, a myosin V from Saccharomyces cerevisiae. This structure, combined with FRET distance measurements between probes in various CaM-IQ complexes, comparative sequence analysis, and the previously determined structures of Mlc1p-IQ2 and Mlc1p-IQ4, allowed building a model of the LCBD of myosin V. The IQs of myosin V are distributed into three pairs. There appear to be specific cooperative interactions between light chains within each IQ pair, but little or no interaction between pairs, providing flexibility at their junctions. The second and third IQ pairs each present a light chain, whether CaM or a CaM-related molecule, bound in a noncanonical extended conformation in which the N-lobe does not interact with the IQ motif. The resulting free N-lobes may engage in protein-protein interactions. The extended conformation is characteristic of the single IQ of myosin VI and is common throughout the myosin superfamily. The model points to a prominent role of the LCBD in the function, regulation, and molecular interactions of myosin V.
-
-	Structure of the light chain-binding domain of myosin V.,Terrak M, Rebowski G, Lu RC, Grabarek Z, Dominguez R Proc Natl Acad Sci U S A. 2005 Sep 6;102(36):12718-23. Epub 2005 Aug 24. PMID:16120677<ref>PMID:16120677</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1n2d" 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: ~~Lu, R C~~]]	+	[[Category: Saccharomyces cerevisiae S288C]]
-	[[Category: ~~Stafford, W F~~]]	+	[[Category: Dominguez R]]
-	[[Category: ~~Terrak, M~~]]	+	[[Category: Lu RC]]
-	[[Category: ~~Wu, G~~]]	+	[[Category: Stafford WF]]
-	[[Category: ~~Cell cycle~~]]	+	[[Category: Terrak M]]
-	[[Category: ~~Iq motif]]~~	+	[[Category: Wu G]]
-	~~[[Category: Myosin light chain]]~~	+
-	~~[[Category: Protein-peptide complex~~]]	+

OCA at 08:43, 2 December 2020

OCA — Wed, 02 Dec 2020 08:43:57 GMT

←Older revision		Revision as of 08:43, 2 December 2020
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	==Ternary complex of MLC1P bound to IQ2 and IQ3 of Myo2p, a class V myosin==		==Ternary complex of MLC1P bound to IQ2 and IQ3 of Myo2p, a class V myosin==
-	<StructureSection load='1n2d' size='340' side='right' caption='[[1n2d]], [[Resolution\|resolution]] 2.00Å' scene=''>	+	<StructureSection load='1n2d' size='340' side='right'caption='[[1n2d]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1n2d]] is a 3 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=1N2D OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1N2D FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1n2d]] is a 3 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=1N2D OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1N2D FirstGlance]. <br>
-	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1m45\|1m45]], [[1m46\|1m46]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1m45\|1m45]], [[1m46\|1m46]]</div></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='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'>[http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1n2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n2d OCA], [http://pdbe.org/1n2d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1n2d RCSB], [http://www.ebi.ac.uk/pdbsum/1n2d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1n2d 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=1n2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n2d OCA], [http://pdbe.org/1n2d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1n2d RCSB], [http://www.ebi.ac.uk/pdbsum/1n2d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1n2d ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/n2/1n2d_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/n2/1n2d_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>
Line 29:		Line 29:
	</div>		</div>
	<div class="pdbe-citations 1n2d" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1n2d" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Myosin 3D Structures\|Myosin 3D Structures]]
	== References ==		== References ==
	<references/>		<references/>
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	</StructureSection>		</StructureSection>
	[[Category: Atcc 18824]]		[[Category: Atcc 18824]]
		+	[[Category: Large Structures]]
	[[Category: Dominguez, R]]		[[Category: Dominguez, R]]
	[[Category: Lu, R C]]		[[Category: Lu, R C]]

OCA at 10:07, 12 October 2017

OCA — Thu, 12 Oct 2017 10:07:23 GMT

←Older revision		Revision as of 10:07, 12 October 2017
Line 1:		Line 1:
		+
	==Ternary complex of MLC1P bound to IQ2 and IQ3 of Myo2p, a class V myosin==		==Ternary complex of MLC1P bound to IQ2 and IQ3 of Myo2p, a class V myosin==
	<StructureSection load='1n2d' size='340' side='right' caption='[[1n2d]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='1n2d' size='340' side='right' caption='[[1n2d]], [[Resolution\|resolution]] 2.00Å' scene=''>
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	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1m45\|1m45]], [[1m46\|1m46]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1m45\|1m45]], [[1m46\|1m46]]</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='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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1n2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n2d OCA], [http://pdbe.org/1n2d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1n2d RCSB], [http://www.ebi.ac.uk/pdbsum/1n2d PDBsum]</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=1n2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n2d OCA], [http://pdbe.org/1n2d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1n2d RCSB], [http://www.ebi.ac.uk/pdbsum/1n2d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1n2d ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	</div>		</div>
	<div class="pdbe-citations 1n2d" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1n2d" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Myosin\|Myosin]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 12:08, 7 February 2016

OCA — Sun, 07 Feb 2016 12:08:13 GMT

←Older revision		Revision as of 12:08, 7 February 2016
Line 17:		Line 17:
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</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].	+	</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=1n2d ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 01:21, 10 September 2015

OCA — Thu, 10 Sep 2015 01:21:51 GMT

←Older revision		Revision as of 01:21, 10 September 2015
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	<StructureSection load='1n2d' size='340' side='right' caption='[[1n2d]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='1n2d' size='340' side='right' caption='[[1n2d]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1n2d]] is a 3 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=1N2D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1N2D FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1n2d]] is a 3 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=1N2D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1N2D FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1m45\|1m45]], [[1m46\|1m46]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1m45\|1m45]], [[1m46\|1m46]]</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 ~~Saccharomyces cerevisiae~~])</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1n2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n2d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1n2d RCSB], [http://www.ebi.ac.uk/pdbsum/1n2d PDBsum]</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=1n2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n2d OCA], [http://pdbe.org/1n2d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1n2d RCSB], [http://www.ebi.ac.uk/pdbsum/1n2d PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 1n2d" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 34:		Line 35:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Saccharomyces cerevisiae~~]]	+	[[Category: Atcc 18824]]
	[[Category: Dominguez, R]]		[[Category: Dominguez, R]]
	[[Category: Lu, R C]]		[[Category: Lu, R C]]

OCA at 14:57, 24 December 2014

OCA — Wed, 24 Dec 2014 14:57:42 GMT

←Older revision		Revision as of 14:57, 24 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1n2d]] is a 3 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=1N2D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1N2D FirstGlance]. <br>		<table><tr><td colspan='2'>[[1n2d]] is a 3 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=1N2D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1N2D FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1m45\|1m45]], [[1m46\|1m46]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1m45\|1m45]], [[1m46\|1m46]]</td></tr>
-	<tr><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 Saccharomyces cerevisiae])</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 Saccharomyces cerevisiae])</td></tr>
-	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1n2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n2d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1n2d RCSB], [http://www.ebi.ac.uk/pdbsum/1n2d PDBsum]</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=1n2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n2d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1n2d RCSB], [http://www.ebi.ac.uk/pdbsum/1n2d PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== 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>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 33:		Line 35:
	</StructureSection>		</StructureSection>
	[[Category: Saccharomyces cerevisiae]]		[[Category: Saccharomyces cerevisiae]]
-	[[Category: Dominguez, R.]]	+	[[Category: Dominguez, R]]
-	[[Category: Lu, R C.]]	+	[[Category: Lu, R C]]
-	[[Category: Stafford, W F.]]	+	[[Category: Stafford, W F]]
-	[[Category: Terrak, M.]]	+	[[Category: Terrak, M]]
-	[[Category: Wu, G.]]	+	[[Category: Wu, G]]
	[[Category: Cell cycle]]		[[Category: Cell cycle]]
	[[Category: Iq motif]]		[[Category: Iq motif]]
	[[Category: Myosin light chain]]		[[Category: Myosin light chain]]
	[[Category: Protein-peptide complex]]		[[Category: Protein-peptide complex]]

OCA at 15:52, 28 September 2014

OCA — Sun, 28 Sep 2014 15:52:27 GMT

←Older revision		Revision as of 15:52, 28 September 2014
Line 1:		Line 1:
-	[[~~Image:~~1n2d.~~png~~\|~~left~~\|200px]]	+	==Ternary complex of MLC1P bound to IQ2 and IQ3 of Myo2p, a class V myosin==
		+	<StructureSection load='1n2d' size='340' side='right' caption='[[1n2d]], [[Resolution\|resolution]] 2.00Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1n2d]] is a 3 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=1N2D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1N2D FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1m45\|1m45]], [[1m46\|1m46]]</td></tr>
		+	<tr><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 Saccharomyces cerevisiae])</td></tr>
		+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1n2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n2d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1n2d RCSB], [http://www.ebi.ac.uk/pdbsum/1n2d PDBsum]</span></td></tr>
		+	<table>
		+	== Evolutionary Conservation ==
		+	[[Image:Consurf_key_small.gif\|200px\|right]]
		+	Check<jmol>
		+	<jmolCheckbox>
		+	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/n2/1n2d_consurf.spt"</scriptWhenChecked>
		+	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
		+	<text>to colour the structure by Evolutionary Conservation</text>
		+	</jmolCheckbox>
		+	</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].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Myosin V is a double-headed molecular motor involved in organelle transport. Two distinctive features of this motor, processivity and the ability to take extended linear steps of approximately 36 nm along the actin helical track, depend on its unusually long light chain-binding domain (LCBD). The LCBD of myosin V consists of six tandem IQ motifs, which constitute the binding sites for calmodulin (CaM) and CaM-like light chains. Here, we report the 2-A resolution crystal structure of myosin light chain 1 (Mlc1p) bound to the IQ2-IQ3 fragment of Myo2p, a myosin V from Saccharomyces cerevisiae. This structure, combined with FRET distance measurements between probes in various CaM-IQ complexes, comparative sequence analysis, and the previously determined structures of Mlc1p-IQ2 and Mlc1p-IQ4, allowed building a model of the LCBD of myosin V. The IQs of myosin V are distributed into three pairs. There appear to be specific cooperative interactions between light chains within each IQ pair, but little or no interaction between pairs, providing flexibility at their junctions. The second and third IQ pairs each present a light chain, whether CaM or a CaM-related molecule, bound in a noncanonical extended conformation in which the N-lobe does not interact with the IQ motif. The resulting free N-lobes may engage in protein-protein interactions. The extended conformation is characteristic of the single IQ of myosin VI and is common throughout the myosin superfamily. The model points to a prominent role of the LCBD in the function, regulation, and molecular interactions of myosin V.

-	~~{{STRUCTURE_1n2d\| PDB=1n2d \| SCENE= }}~~	+	Structure of the light chain-binding domain of myosin V.,Terrak M, Rebowski G, Lu RC, Grabarek Z, Dominguez R Proc Natl Acad Sci U S A. 2005 Sep 6;102(36):12718-23. Epub 2005 Aug 24. PMID:16120677<ref>PMID:16120677</ref>

-	~~===Ternary complex of MLC1P bound to IQ2 and IQ3 of Myo2p~~, a ~~class V myosin===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_16120677}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[1n2d]] is a 3 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=1N2D OCA].~~	+

	==See Also==		==See Also==
	*[[Myosin\|Myosin]]		*[[Myosin\|Myosin]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:016120677<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Saccharomyces cerevisiae]]		[[Category: Saccharomyces cerevisiae]]
	[[Category: Dominguez, R.]]		[[Category: Dominguez, R.]]

OCA at 06:35, 20 October 2012

OCA — Sat, 20 Oct 2012 06:35:37 GMT

←Older revision		Revision as of 06:35, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[1n2d]] is a 3 chain structure ~~of [[Myosin]]~~ 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=1N2D OCA].	+	[[1n2d]] is a 3 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=1N2D OCA].

	==See Also==		==See Also==

OCA at 13:41, 25 July 2012

OCA — Wed, 25 Jul 2012 13:41:09 GMT

←Older revision		Revision as of 13:41, 25 July 2012
Line 1:		Line 1:
	[[Image:1n2d.png\|left\|200px]]		[[Image:1n2d.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_1n2d", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	or leave the SCENE parameter empty for the default display.
-	-->
	{{STRUCTURE_1n2d\| PDB=1n2d \| SCENE= }}		{{STRUCTURE_1n2d\| PDB=1n2d \| SCENE= }}

	===Ternary complex of MLC1P bound to IQ2 and IQ3 of Myo2p, a class V myosin===		===Ternary complex of MLC1P bound to IQ2 and IQ3 of Myo2p, a class V myosin===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_16120677}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 16120677 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_16120677}}		{{ABSTRACT_PUBMED_16120677}}

Line 22:		Line 11:

	==See Also==		==See Also==
-	*[[Myosin]]	+	*[[Myosin\|Myosin]]

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~16120677~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:016120677</ref><references group="xtra"/>
	[[Category: Saccharomyces cerevisiae]]		[[Category: Saccharomyces cerevisiae]]
	[[Category: Dominguez, R.]]		[[Category: Dominguez, R.]]

OCA: Protected "1n2d" [edit=sysop:move=sysop]

OCA — Mon, 27 Dec 2010 00:50:49 GMT

Protected "1n2d" [edit=sysop:move=sysop]

←Older revision

Revision as of 00:50, 27 December 2010