9mfy

Motor domain-Pac1 complex with ADP AAA1 and Apo AAA3 from yeast full-length dynein-1 and Pac1 in 0.1 mM ATP condition

spinqualitylabelsall models 9mfy, resolution 3.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9mfy is a 2 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.3Å Ligands: ADP, ATP, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function LIS1_YEAST Positively regulates the activity of the minus-end directed microtubule motor protein dynein. Plays a central role in positioning the mitotic spindle at the bud neck during cell division. Targets cytoplasmic dynein to microtubule plus ends, thereby promoting dynein-mediated microtubule sliding along the bud cortex and consequently the movement of the mitotic spindle to the bud neck. Following plus end binding, dynein may be offloaded to the cortex by NUM1. Required for viability in the absence of the kinesin-related microtubule-dependent motor protein CIN8.[HAMAP-Rule:MF_03141]

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