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3j8y

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Revision as of 03:15, 25 December 2014

High-resolution structure of ATP analog-bound kinesin on microtubules

Structural highlights

3j8y is a 3 chain structure with sequence from [1] and Sus scrofa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , ,
Related:	3j8x
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[KINH_HUMAN] Microtubule-dependent motor required for normal distribution of mitochondria and lysosomes (By similarity). [F2Z5B2_PIG] Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain.[RuleBase:RU003505] [TBA1B_PIG] Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain.

Publication Abstract from PubMed

Microtubule-based transport by the kinesin motors, powered by ATP hydrolysis, is essential for a wide range of vital processes in eukaryotes. We obtained insight into this process by developing atomic models for no-nucleotide and ATP states of the monomeric kinesin motor domain on microtubules from cryo-EM reconstructions at 5-6A resolution. By comparing these models with existing X-ray structures of ADP-bound kinesin, we infer a mechanistic scheme in which microtubule attachment, mediated by a universally conserved 'linchpin' residue in kinesin (N255), triggers a clamshell opening of the nucleotide cleft and accompanying release of ADP. Binding of ATP re-closes the cleft in a manner that tightly couples to translocation of cargo, via kinesin's 'neck linker' element. These structural transitions are reminiscent of the analogous nucleotide-exchange steps in the myosin and F1-ATPase motors, and inform how the two heads of a kinesin dimer 'gate' each other to promote coordinated stepping along microtubules.

High-resolution structures of kinesin on microtubules provide a basis for nucleotide-gated force generation.,Shang Z, Zhou K, Xu C, Csencsits R, Cochran JC, Sindelar CV Elife. 2014 Nov 21;3. doi: 10.7554/eLife.04686. PMID:25415053^[1]

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

References

↑ Shang Z, Zhou K, Xu C, Csencsits R, Cochran JC, Sindelar CV. High-resolution structures of kinesin on microtubules provide a basis for nucleotide-gated force generation. Elife. 2014 Nov 21;3. doi: 10.7554/eLife.04686. PMID:25415053 doi:http://dx.doi.org/10.7554/eLife.04686

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/3j8y"

@@ Line 7: / Line 7: @@
 <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=3j8y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j8y OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3j8y RCSB], [http://www.ebi.ac.uk/pdbsum/3j8y 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). [[http://www.uniprot.org/uniprot/F2Z5B2_PIG F2Z5B2_PIG]] Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain.[RuleBase:RU003505] [[http://www.uniprot.org/uniprot/TBA1B_PIG TBA1B_PIG]] Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

3j8y

From Proteopedia

Revision as of 03:15, 25 December 2014

High-resolution structure of ATP analog-bound kinesin on microtubules

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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