6kio

Complex of yeast cytoplasmic dynein MTBD-High and MT without DTT

Loading... Status: waiting for Mol* initialization Structural highlights 6kio is a 3 chain structure with sequence from Saccharomyces cerevisiae S288C and Sus scrofa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.94Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function 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. Publication Abstract from PubMed The movements of cytoplasmic dynein on microtubule (MT) tracks is achieved by two-way communication between the microtubule-binding domain (MTBD) and the ATPase domain via a coiled-coil stalk, but the structural basis of this communication remains elusive. Here, we regulate MTBD either in high-affinity or low-affinity states by introducing a disulfide bond to the stalk and analyze the resulting structures by NMR and cryo-EM. In the MT-unbound state, the affinity changes of MTBD are achieved by sliding of the stalk alpha-helix by a half-turn, which suggests that structural changes propagate from the ATPase-domain to MTBD. In addition, MT binding induces further sliding of the stalk alpha-helix even without the disulfide bond, suggesting how the MT-induced conformational changes propagate toward the ATPase domain. Based on differences in the MT-binding surface between the high- and low-affinity states, we propose a potential mechanism for the directional bias of dynein movement on MT tracks. Structural basis for two-way communication between dynein and microtubules.,Nishida N, Komori Y, Takarada O, Watanabe A, Tamura S, Kubo S, Shimada I, Kikkawa M Nat Commun. 2020 Feb 25;11(1):1038. doi: 10.1038/s41467-020-14842-8. PMID:32098965 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Dynein 3D structures Tubulin 3D Structures

Proteopedia Page Contributors and Editors (what is this?)

OCA