3j8y | pdb_00003j8y

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

spinqualitylabelsall models 3j8y, resolution 5.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D 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: ATP, GDP, GTP, MG Related: 3j8x Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Tubulin

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