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4lnu

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Revision as of 05:04, 25 December 2014

Nucleotide-free kinesin motor domain in complex with tubulin and a DARPin

Structural highlights

4lnu is a 4 chain structure with sequence from [1] and Ovis aries. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , , , ,
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[KINH_HUMAN] Microtubule-dependent motor required for normal distribution of mitochondria and lysosomes (By similarity).

Publication Abstract from PubMed

Kinesin-1 is a dimeric ATP-dependent motor protein that moves towards microtubules (+) ends. This movement is driven by two conformations (docked and undocked) of the two motor domains carboxy-terminal peptides (named neck linkers), in correlation with the nucleotide bound to each motor domain. Despite extensive data on kinesin-1, the structural connection between its nucleotide cycle and movement has remained elusive, mostly because the structure of the critical tubulin-bound apo-kinesin state was unknown. Here we report the 2.2 A structure of this complex. From its comparison with detached kinesin-ADP and tubulin-bound kinesin-ATP, we identify three kinesin motor subdomains that move rigidly along the nucleotide cycle. Our data reveal how these subdomains reorient on binding to tubulin and when ATP binds, leading respectively to ADP release and to neck linker docking. These results establish a framework for understanding the transformation of chemical energy into mechanical work by (+) end-directed kinesins.

The structure of apo-kinesin bound to tubulin links the nucleotide cycle to movement.,Cao L, Wang W, Jiang Q, Wang C, Knossow M, Gigant B Nat Commun. 2014 Nov 14;5:5364. doi: 10.1038/ncomms6364. PMID:25395082^[1]

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

References

↑ Cao L, Wang W, Jiang Q, Wang C, Knossow M, Gigant B. The structure of apo-kinesin bound to tubulin links the nucleotide cycle to movement. Nat Commun. 2014 Nov 14;5:5364. doi: 10.1038/ncomms6364. PMID:25395082 doi:http://dx.doi.org/10.1038/ncomms6364

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/4lnu"

@@ Line 6: / Line 6: @@
 <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=4lnu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lnu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4lnu RCSB], [http://www.ebi.ac.uk/pdbsum/4lnu PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/KINH_HUMAN KINH_HUMAN]] Microtubule-dependent motor required for normal distribution of mitochondria and lysosomes (By similarity).
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

4lnu

From Proteopedia

Revision as of 05:04, 25 December 2014

Nucleotide-free kinesin motor domain in complex with tubulin and a DARPin

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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