1f9v: Difference between revisions

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New page: left|200px<br /><applet load="1f9v" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f9v, resolution 1.3Å" /> '''CRYSTAL STRUCTURES OF...
 
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[[Image:1f9v.gif|left|200px]]<br /><applet load="1f9v" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1f9v, resolution 1.3&Aring;" />
'''CRYSTAL STRUCTURES OF MUTANTS REVEAL A SIGNALLING PATHWAY FOR ACTIVATION OF THE KINESIN MOTOR ATPASE'''<br />


==Overview==
==CRYSTAL STRUCTURES OF MUTANTS REVEAL A SIGNALLING PATHWAY FOR ACTIVATION OF THE KINESIN MOTOR ATPASE==
Molecular motors move along actin or microtubules by rapidly hydrolyzing, ATP and undergoing changes in filament-binding affinity with steps of the, nucleotide hydrolysis cycle. It is generally accepted that motor binding, to its filament greatly increases the rate of ATP hydrolysis, but the, structural changes in the motor associated with ATPase activation are not, known. To identify the conformational changes underlying motor movement on, its filament, we solved the crystal structures of three kinesin mutants, that decouple nucleotide and microtubule binding by the motor, and block, microtubule-activated, but not basal, ATPase activity. Conformational, changes in the structures include a disordered loop and helices in the, switch I region and a visible switch II loop, which is disordered in, wild-type structures. Switch I moved closer to the bound nucleotide in two, mutant structures, perturbing water-mediated interactions with the Mg2+., This could weaken Mg2+ binding and accelerate ADP release to activate the, motor ATPASE: The structural changes we observe define a signaling pathway, within the motor for ATPase activation that is likely to be essential for, motor movement on microtubules.
<StructureSection load='1f9v' size='340' side='right'caption='[[1f9v]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1f9v]] 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=1F9V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F9V FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.3&#8491;</td></tr>
<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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1f9v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f9v OCA], [https://pdbe.org/1f9v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f9v RCSB], [https://www.ebi.ac.uk/pdbsum/1f9v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f9v ProSAT]</span></td></tr>
</table>
== Function ==
[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>
== 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/f9/1f9v_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/main_output.php?pdb_ID=1f9v ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1F9V 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=1F9V OCA].
*[[Kinesin 3D Structures|Kinesin 3D Structures]]
 
== References ==
==Reference==
<references/>
A structural pathway for activation of the kinesin motor ATPase., Yun M, Zhang X, Park CG, Park HW, Endow SA, EMBO J. 2001 Jun 1;20(11):2611-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11387196 11387196]
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Endow SA]]
[[Category: Endow, S.A.]]
[[Category: Park CG]]
[[Category: Park, C.G.]]
[[Category: Park HW]]
[[Category: Park, H.W.]]
[[Category: Yun M]]
[[Category: Yun, M.]]
[[Category: Zhang X]]
[[Category: Zhang, X.]]
[[Category: ADP]]
[[Category: MG]]
[[Category: kar3]]
[[Category: kinesin-related protein]]
[[Category: microtubinding proteinbule]]
[[Category: motor protein]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:44:43 2007''

Latest revision as of 10:12, 7 February 2024

CRYSTAL STRUCTURES OF MUTANTS REVEAL A SIGNALLING PATHWAY FOR ACTIVATION OF THE KINESIN MOTOR ATPASECRYSTAL STRUCTURES OF MUTANTS REVEAL A SIGNALLING PATHWAY FOR ACTIVATION OF THE KINESIN MOTOR ATPASE

Structural highlights

1f9v is a 1 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.3Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.[1] [2]

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. ↑ Meluh PB, Rose MD. KAR3, a kinesin-related gene required for yeast nuclear fusion. Cell. 1990 Mar 23;60(6):1029-41. PMID:2138512
  2. ↑ Shanks RM, Kamieniecki RJ, Dawson DS. The Kar3-interacting protein Cik1p plays a critical role in passage through meiosis I in Saccharomyces cerevisiae. Genetics. 2001 Nov;159(3):939-51. PMID:11729143

1f9v, resolution 1.30Å

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