2o0a

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{{Seed}}
 
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[[Image:2o0a.png|left|200px]]
 
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==The structure of the C-terminal domain of Vik1 has a motor domain fold but lacks a nucleotide-binding site.==
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The line below this paragraph, containing "STRUCTURE_2o0a", creates the "Structure Box" on the page.
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<StructureSection load='2o0a' size='340' side='right'caption='[[2o0a]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2o0a]] 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=2O0A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2O0A FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 1.6&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
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{{STRUCTURE_2o0a| PDB=2o0a | SCENE= }}
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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=2o0a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o0a OCA], [https://pdbe.org/2o0a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2o0a RCSB], [https://www.ebi.ac.uk/pdbsum/2o0a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2o0a ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/VIK1_YEAST VIK1_YEAST] Targets and/or maintains KAR3 at the spindle pole body during vegetative growth.<ref>PMID:10087265</ref> <ref>PMID:11729143</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/o0/2o0a_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=2o0a ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Conventional kinesin and class V and VI myosins coordinate the mechanochemical cycles of their motor domains for processive movement of cargo along microtubules or actin filaments. It is widely accepted that this coordination is achieved by allosteric communication or mechanical strain between the motor domains, which controls the nucleotide state and interaction with microtubules or actin. However, questions remain about the interplay between the strain and the nucleotide state. We present an analysis of Saccharomyces cerevisiae Kar3/Vik1, a heterodimeric C-terminal Kinesin-14 containing catalytic Kar3 and the nonmotor protein Vik1. The X-ray crystal structure of Vik1 exhibits a similar fold to the kinesin and myosin catalytic head, but lacks an ATP binding site. Vik1 binds more tightly to microtubules than Kar3 and facilitates cooperative microtubule decoration by Kar3/Vik1 heterodimers, and yet allows motility. These results demand communication between Vik1 and Kar3 via a mechanism that coordinates their interactions with microtubules.
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===The structure of the C-terminal domain of Vik1 has a motor domain fold but lacks a nucleotide-binding site.===
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Vik1 modulates microtubule-Kar3 interactions through a motor domain that lacks an active site.,Allingham JS, Sproul LR, Rayment I, Gilbert SP Cell. 2007 Mar 23;128(6):1161-72. PMID:17382884<ref>PMID:17382884</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_17382884}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2o0a" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 17382884 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_17382884}}
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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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2O0A is a [[Single protein]] structure of 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=2O0A OCA].
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==Reference==
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Vik1 modulates microtubule-Kar3 interactions through a motor domain that lacks an active site., Allingham JS, Sproul LR, Rayment I, Gilbert SP, Cell. 2007 Mar 23;128(6):1161-72. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17382884 17382884]
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Single protein]]
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[[Category: Allingham JS]]
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[[Category: Allingham, J S.]]
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[[Category: Gilbert SP]]
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[[Category: Gilbert, S P.]]
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[[Category: Rayment I]]
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[[Category: Rayment, I.]]
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[[Category: Sproul LR]]
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[[Category: Sproul, L R.]]
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[[Category: Heterodimer]]
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[[Category: Kinesin]]
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[[Category: Kinesin-14]]
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[[Category: Microtubule-binding]]
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[[Category: Motor domain]]
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[[Category: Motor homology domain]]
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[[Category: Vik1]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 22:47:01 2008''
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Current revision

The structure of the C-terminal domain of Vik1 has a motor domain fold but lacks a nucleotide-binding site.

PDB ID 2o0a

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