6ugf | pdb_00006ugf

Katanin hexamer in the ring conformation with resolved protomer one in complex with substrate

spinqualitylabelsall models 6ugf, resolution 4.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6ugf is a 7 chain structure with sequence from Caeel. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ATP, MG Gene: mei-1, T01G9.5 (CAEEL) Activity: Microtubule-severing ATPase, with EC number 5.6.1.1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [KTNA1_CAEEL] Catalytic subunit of a complex which severs microtubules in an ATP-dependent manner. Microtubule severing may promote rapid reorganization of cellular microtubule arrays. Required specifically for meiotic spindle formation in the female germline; the presence of this protein is inimical to the formation of mitotic spindles (PubMed:8027178, PubMed:10809666, PubMed:12885567). In body wall muscles, regulates organization of myosin thick filaments (PubMed:22621901).[HAMAP-Rule:MF_03023] Publication Abstract from PubMed The AAA ATPase katanin severs microtubules. It is critical in cell division, centriole biogenesis, and neuronal morphogenesis. Its mutation causes microcephaly. The microtubule templates katanin hexamerization and activates its ATPase. The structural basis for these activities and how they lead to severing is unknown. Here, we show that beta-tubulin tails are necessary and sufficient for severing. Cryoelectron microscopy (cryo-EM) structures reveal the essential tubulin tail glutamates gripped by a double spiral of electropositive loops lining the katanin central pore. Each spiral couples allosterically to the ATPase and binds alternating, successive substrate residues, with consecutive residues coordinated by adjacent protomers. This tightly couples tail binding, hexamerization, and ATPase activation. Hexamer structures in different states suggest an ATPase-driven, ratchet-like translocation of the tubulin tail through the pore. A disordered region outside the AAA core anchors katanin to the microtubule while the AAA motor exerts the forces that extract tubulin dimers and sever the microtubule. Katanin Grips the beta-Tubulin Tail through an Electropositive Double Spiral to Sever Microtubules.,Zehr EA, Szyk A, Szczesna E, Roll-Mecak A Dev Cell. 2019 Nov 8. pii: S1534-5807(19)30854-8. doi:, 10.1016/j.devcel.2019.10.010. PMID:31735665 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA