2hxf

KIF1A head-microtubule complex structure in amppnp-form

spinqualitylabelsall models 2hxf, resolution 10.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2hxf is a 3 chain structure with sequence from Lk3 transgenic mice and Sus scrofa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ANP, GDP, GTP, MG, TA1 Related: 1jff, 1i5s, 1ia0, 2hxh Gene: Kif1a (LK3 transgenic mice) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [TBA1A_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. [KIF1A_MOUSE] Motor for anterograde axonal transport of synaptic vesicle precursors. [TBB_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. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Kinesin is an ATP-driven microtubule (MT)-based motor fundamental to organelle transport. Although a number of kinesin crystal structures have been solved, the structural evidence for coupling between the bound nucleotide and the conformation of kinesin is elusive. In addition, the structural basis of the MT-induced ATPase activity of kinesin is not clear because of the absence of the MT in the structure. Here, we report cryo-electron microscopy structures of the monomeric kinesin KIF1A-MT complex in two nucleotide states at about 10 A resolution, sufficient to reveal the secondary structure. These high-resolution maps visualized clear structural changes that suggest a mechanical pathway from the nucleotide to the neck linker via the motor core rotation. In addition, new nucleotide binding pocket conformations are observed that are different from X-ray crystallographic structures; it is closed in the 5'-adenylyl-imidodiphosphate state, but open in the ADP state. These results suggest a structural model of biased diffusion movement of monomeric kinesin motor. High-resolution cryo-EM maps show the nucleotide binding pocket of KIF1A in open and closed conformations.,Kikkawa M, Hirokawa N EMBO J. 2006 Sep 20;25(18):4187-94. Epub 2006 Aug 31. PMID:16946706 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Kinesin 3D Structures Tubulin

Proteopedia Page Contributors and Editors (what is this?)

OCA