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2o0a

From Proteopedia

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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.

Structural highlights

2o0a 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 1.6Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

VIK1_YEAST Targets and/or maintains KAR3 at the spindle pole body during vegetative growth.^[1] ^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Manning BD, Barrett JG, Wallace JA, Granok H, Snyder M. Differential regulation of the Kar3p kinesin-related protein by two associated proteins, Cik1p and Vik1p. J Cell Biol. 1999 Mar 22;144(6):1219-33. PMID:10087265
↑ 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
↑ Allingham JS, Sproul LR, Rayment I, Gilbert SP. Vik1 modulates microtubule-Kar3 interactions through a motor domain that lacks an active site. Cell. 2007 Mar 23;128(6):1161-72. PMID:17382884 doi:10.1016/j.cell.2006.12.046

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2o0a"

@@ Line 1: / Line 1: @@
 ==The structure of the C-terminal domain of Vik1 has a motor domain fold but lacks a nucleotide-binding site.==
-<StructureSection load='2o0a' size='340' side='right' caption='[[2o0a]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
+<StructureSection load='2o0a' size='340' side='right'caption='[[2o0a]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2o0a]] 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=2O0A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2O0A FirstGlance]. <br>
+<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>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></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]] 1.6&#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=2o0a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o0a OCA], [http://pdbe.org/2o0a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2o0a RCSB], [http://www.ebi.ac.uk/pdbsum/2o0a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2o0a ProSAT]</span></td></tr>
+<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>
+<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>
 </table>
 == Function ==
-[[http://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>
+[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>
 == 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/o0/2o0a_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o0/2o0a_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 32: / Line 33: @@
 __TOC__
 </StructureSection>
-[[Category: Atcc 18824]]
+[[Category: Large Structures]]
-[[Category: Allingham, J S]]
+[[Category: Saccharomyces cerevisiae]]
-[[Category: Gilbert, S P]]
+[[Category: Allingham JS]]
-[[Category: Rayment, I]]
+[[Category: Gilbert SP]]
-[[Category: Sproul, L R]]
+[[Category: Rayment I]]
-[[Category: Cell cycle-transport protein complex]]
+[[Category: Sproul LR]]
-[[Category: Heterodimer]]
-[[Category: Kinesin]]
-[[Category: Kinesin-14]]
-[[Category: Microtubule-binding]]
-[[Category: Motor domain]]
-[[Category: Motor homology domain]]
-[[Category: Vik1]]

2o0a

From Proteopedia

Current revision

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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