7a40

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Nucleotide-free OSM-3 kinesin motor domain

Structural highlights

7a40 is a 2 chain structure with sequence from Caenorhabditis elegans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.297Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

OSM3_CAEEL Kinesin motor protein which is required for the anterograde intraflagellar transport (IFT) along the middle segment of the sensory neuron cilia together with the kinesin II motor complex (composed of klp-11, klp-20 and kap-1) and on its own, is required for IFT along the distal segment (PubMed:17000880, PubMed:17420466). In addition, regulates the length of cilia (PubMed:17420466). May have a role during neurogenesis and axonal transport (PubMed:7714894, PubMed:7690265).^[1] ^[2] ^[3] ^[4]

Publication Abstract from PubMed

Motile kinesins are motor proteins that translocate along microtubules as they hydrolyze ATP. They share a conserved motor domain which harbors both ATPase and microtubule-binding activities. An ATP hydrolysis mechanism involving two water molecules has been proposed based on the structure of the kinesin-5 Eg5 bound to an ATP analog. Whether this mechanism is general in the kinesin superfamily remains uncertain. Here, we present structural snapshots of the motor domain of OSM-3 along its nucleotide cycle. OSM-3 belongs to the homodimeric kinesin-2 subfamily and is the Caenorhabditis elegans homologue of human KIF17. OSM-3 bound to ADP or devoid of a nucleotide shows features of ADP-kinesins with a docked neck linker. When bound to an ATP analog, OSM-3 adopts a conformation similar to those of several ATP-like kinesins, either isolated or bound to tubulin. Moreover, the OSM-3 nucleotide-binding site is virtually identical to that of ATP-like Eg5, demonstrating a shared ATPase mechanism. Therefore, our data extend to kinesin-2 the two-water ATP hydrolysis mechanism and further suggest that it is universal within the kinesin superfamily. PROTEIN DATABASE ENTRIES: 7A3Z, 7A40, 7A5E.

Structural snapshots of the kinesin-2 OSM-3 along its nucleotide cycle: implications for the ATP hydrolysis mechanism.,Varela PF, Chenon M, Velours C, Verhey KJ, Menetrey J, Gigant B FEBS Open Bio. 2021 Mar;11(3):564-577. doi: 10.1002/2211-5463.13101. Epub 2021 , Feb 28. PMID:33513284^[5]

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

References

↑ Pan X, Ou G, Civelekoglu-Scholey G, Blacque OE, Endres NF, Tao L, Mogilner A, Leroux MR, Vale RD, Scholey JM. Mechanism of transport of IFT particles in C. elegans cilia by the concerted action of kinesin-II and OSM-3 motors. J Cell Biol. 2006 Sep 25;174(7):1035-45. PMID:17000880 doi:10.1083/jcb.200606003
↑ Burghoorn J, Dekkers MP, Rademakers S, de Jong T, Willemsen R, Jansen G. Mutation of the MAP kinase DYF-5 affects docking and undocking of kinesin-2 motors and reduces their speed in the cilia of Caenorhabditis elegans. Proc Natl Acad Sci U S A. 2007 Apr 24;104(17):7157-62. PMID:17420466 doi:10.1073/pnas.0606974104
↑ Shakir MA, Fukushige T, Yasuda H, Miwa J, Siddiqui SS. C. elegans osm-3 gene mediating osmotic avoidance behaviour encodes a kinesin-like protein. Neuroreport. 1993 Jul;4(7):891-4. PMID:7690265 doi:10.1097/00001756-199307000-00013
↑ Tabish M, Siddiqui ZK, Nishikawa K, Siddiqui SS. Exclusive expression of C. elegans osm-3 kinesin gene in chemosensory neurons open to the external environment. J Mol Biol. 1995 Mar 31;247(3):377-89. PMID:7714894 doi:10.1006/jmbi.1994.0146
↑ Varela PF, Chenon M, Velours C, Verhey KJ, Ménétrey J, Gigant B. Structural snapshots of the kinesin-2 OSM-3 along its nucleotide cycle: implications for the ATP hydrolysis mechanism. FEBS Open Bio. 2021 Mar;11(3):564-577. PMID:33513284 doi:10.1002/2211-5463.13101