2f6h: Difference between revisions

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 ==Myosin V cargo binding domain==
-<StructureSection load='2f6h' size='340' side='right' caption='[[2f6h]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
+<StructureSection load='2f6h' size='340' side='right'caption='[[2f6h]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2f6h]] is a 1 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=2F6H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2F6H FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2f6h]] is a 1 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=2F6H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2F6H FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MYO2, CDC66 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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]] 2.25&#8491;</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=2f6h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f6h OCA], [http://pdbe.org/2f6h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2f6h RCSB], [http://www.ebi.ac.uk/pdbsum/2f6h PDBsum]</span></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=2f6h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f6h OCA], [https://pdbe.org/2f6h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2f6h RCSB], [https://www.ebi.ac.uk/pdbsum/2f6h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2f6h ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[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/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 ==
 [[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/f6/2f6h_consurf.spt"</scriptWhenChecked>
+     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f6/2f6h_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].
+</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=2f6h ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Myosin V molecular motors move cargoes on actin filaments. A myosin V may move multiple cargoes to distinct places at different times. The cargoes attach to the globular tail of myosin V via cargo-specific receptors. Here we report the crystal structure at 2.2 A of the myosin V globular tail. The overall tertiary structure has not been previously observed. There are several patches of highly conserved regions distributed on the surface of the tail. These are candidate attachment sites for cargo-specific receptors. Indeed, we identified a region of five conserved surface residues that are solely required for vacuole inheritance. Likewise, we identified a region of five conserved surface residues that are required for secretory vesicle movement, but not vacuole movement. These two regions are at opposite ends of the oblong-shaped cargo-binding domain, and moreover are offset by 180 degrees. The fact that the cargo-binding areas are distant from each other and simultaneously exposed on the surface of the globular tail suggests that major targets for the regulation of cargo attachment are organelle-specific myosin V receptors.
-Structural basis for myosin V discrimination between distinct cargoes.,Pashkova N, Jin Y, Ramaswamy S, Weisman LS EMBO J. 2006 Feb 22;25(4):693-700. Epub 2006 Jan 26. PMID:16437158<ref>PMID:16437158</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 2f6h" style="background-color:#fffaf0;"></div>
 ==See Also==
-*[[Myosin|Myosin]]
+*[[Myosin 3D Structures|Myosin 3D Structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Atcc 18824]]
+[[Category: Large Structures]]
-[[Category: Jin, Y]]
+[[Category: Saccharomyces cerevisiae]]
-[[Category: Pashkova, N]]
+[[Category: Jin Y]]
-[[Category: Ramaswamy, S]]
+[[Category: Pashkova N]]
-[[Category: Weisman, L S]]
+[[Category: Ramaswamy S]]
-[[Category: Cargo binding]]
+[[Category: Weisman LS]]
-[[Category: Cargo transport]]
-[[Category: Mysoin v]]
-[[Category: Secreatory vescile binding]]
-[[Category: Structural protein]]
-[[Category: Vacuole binding]]