4etp

From Proteopedia

(Difference between revisions)

Revision as of 20:31, 25 December 2014

C-terminal motor and motor homology domain of Kar3Vik1 fused to a synthetic heterodimeric coiled coil

Structural highlights

4etp is a 2 chain structure with sequence from Saccharomyces cerevisiae s288c. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , ,
Related:	3kar, 2o0a, 1n6m, 1u0i, 1f9t, 1f9u, 1f9v, 1f9w
Gene:	KAR3, kar3p, P9659.16, YPR141C (Saccharomyces cerevisiae S288c), VIK1, Vik1p, YPL253C (Saccharomyces cerevisiae S288c)
Resources:	FirstGlance, OCA, RCSB, PDBsum

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] [VIK1_YEAST] Targets and/or maintains KAR3 at the spindle pole body during vegetative growth.^[3] ^[4]

Publication Abstract from PubMed

Kinesin-14 motors generate microtubule minus-end-directed force used in mitosis and meiosis. These motors are dimeric and operate with a nonprocessive powerstroke mechanism, but the role of the second head in motility has been unclear. In Saccharomyces cerevisiae, the Kinesin-14 Kar3 forms a heterodimer with either Vik1 or Cik1. Vik1 contains a motor homology domain that retains microtubule binding properties but lacks a nucleotide binding site. In this case, both heads are implicated in motility. Here, we show through structural determination of a C-terminal heterodimeric Kar3Vik1, electron microscopy, equilibrium binding, and motility that at the start of the cycle, Kar3Vik1 binds to or occludes two alphabeta-tubulin subunits on adjacent protofilaments. The cycle begins as Vik1 collides with the microtubule followed by Kar3 microtubule association and ADP release, thereby destabilizing the Vik1-microtubule interaction and positioning the motor for the start of the powerstroke. The results indicate that head-head communication is mediated through the adjoining coiled coil.

Kar3Vik1, a member of the kinesin-14 superfamily, shows a novel kinesin microtubule binding pattern.,Rank KC, Chen CJ, Cope J, Porche K, Hoenger A, Gilbert SP, Rayment I J Cell Biol. 2012 Jun 25;197(7):957-70. doi: 10.1083/jcb.201201132. PMID:22734002^[5]

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

References

↑ Meluh PB, Rose MD. KAR3, a kinesin-related gene required for yeast nuclear fusion. Cell. 1990 Mar 23;60(6):1029-41. PMID:2138512
↑ 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
↑ 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
↑ Rank KC, Chen CJ, Cope J, Porche K, Hoenger A, Gilbert SP, Rayment I. Kar3Vik1, a member of the kinesin-14 superfamily, shows a novel kinesin microtubule binding pattern. J Cell Biol. 2012 Jun 25;197(7):957-70. doi: 10.1083/jcb.201201132. PMID:22734002 doi:10.1083/jcb.201201132

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4etp"

@@ Line 8: / Line 8: @@
 <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=4etp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4etp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4etp RCSB], [http://www.ebi.ac.uk/pdbsum/4etp PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://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>  [[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>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

4etp

From Proteopedia

Revision as of 20:31, 25 December 2014

C-terminal motor and motor homology domain of Kar3Vik1 fused to a synthetic heterodimeric coiled coil

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox