3kar

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(New page: 200px<br /><applet load="3kar" size="450" color="white" frame="true" align="right" spinBox="true" caption="3kar, resolution 2.3&Aring;" /> '''THE MOTOR DOMAIN OF K...)
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[[Image:3kar.jpg|left|200px]]<br /><applet load="3kar" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="3kar, resolution 2.3&Aring;" />
 
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'''THE MOTOR DOMAIN OF KINESIN-LIKE PROTEIN KAR3, A SACCHAROMYCES CEREVISIAE KINESIN-RELATED PROTEIN'''<br />
 
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==Overview==
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==THE MOTOR DOMAIN OF KINESIN-LIKE PROTEIN KAR3, A SACCHAROMYCES CEREVISIAE KINESIN-RELATED PROTEIN==
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The kinesin family of motor proteins, which contain a conserved motor, domain of approximately 350 amino acids, generate movement against, microtubules. Over 90 members of this family have been identified, including motors that move toward the minus or plus end of microtubules., The Kar3 protein from Saccharomyces cerevisiae is a minus end-directed, kinesin family member that is involved in both nuclear fusion, or, karyogamy, and mitosis. The Kar3 protein is 729 residues in length with, the motor domain located in the C-terminal 347 residues. Recently, the, three-dimensional structures of two kinesin family members have been, reported. These structures include the motor domains of the plus, end-directed kinesin heavy chain [Kull, F. J., et al. (1996) Nature 380, 550-555] and the minus end-directed Ncd [Sablin, E. P., et al. (1996), Nature 380, 555-559]. We now report the structure of the Kar3 protein, complexed with Mg.ADP obtained from crystallographic data to 2.3 A. The, structure is similar to those of the earlier kinesin family members, but, shows differences as well, most notably in the length of helix alpha 4, a, helix which is believed to be involved in conformational changes during, the hydrolysis cycle.
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<StructureSection load='3kar' size='340' side='right'caption='[[3kar]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3kar]] 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=3KAR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3KAR FirstGlance]. <br>
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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]] 2.3&#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=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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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=3kar FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kar OCA], [https://pdbe.org/3kar PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3kar RCSB], [https://www.ebi.ac.uk/pdbsum/3kar PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3kar ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/KAR3_YEAST KAR3_YEAST] Essential for yeast nuclear fusion during mating. KAR3 is a bifunctional protein having a kinesin-like motor domain joined to a distinct microtubule binding domain. It may mediate microtubule sliding during nuclear fusion and possibly mitosis. May interact with spindle microtubules to produce an inwardly directed force acting upon the poles. KAR3 function antagonizes CIP8 and KIP1 outward force action. KAR3 motor activity is directed toward the microtubule's minus end.<ref>PMID:2138512</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/ka/3kar_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=3kar ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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3KAR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with MG and ADP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=3KAR OCA].
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*[[Kinesin 3D Structures|Kinesin 3D Structures]]
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== References ==
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==Reference==
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<references/>
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X-ray crystal structure of the yeast Kar3 motor domain complexed with Mg.ADP to 2.3 A resolution., Gulick AM, Song H, Endow SA, Rayment I, Biochemistry. 1998 Feb 17;37(7):1769-76. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9485302 9485302]
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Single protein]]
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[[Category: Endow S]]
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[[Category: Endow, S.]]
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[[Category: Gulick AM]]
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[[Category: Gulick, A.M.]]
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[[Category: Rayment I]]
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[[Category: Rayment, I.]]
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[[Category: Song H]]
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[[Category: Song, H.]]
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[[Category: ADP]]
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[[Category: MG]]
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[[Category: atpase]]
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[[Category: contractile protein]]
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[[Category: kar3]]
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[[Category: kinesin-related protein]]
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[[Category: microtubule binding protein]]
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[[Category: motor protein]]
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[[Category: p-loop]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:48:24 2007''
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Current revision

THE MOTOR DOMAIN OF KINESIN-LIKE PROTEIN KAR3, A SACCHAROMYCES CEREVISIAE KINESIN-RELATED PROTEIN

PDB ID 3kar

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