5mjs | pdb_00005mjs

S. pombe microtubule copolymerized with GTP and Mal3-143

spinqualitylabelsall models 5mjs, resolution 4.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5mjs is a 9 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GDP, GTP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [TBB_SCHPO] 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. [TBA1_SCHPO] 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. [MAL3_SCHPO] May play a role in regulating the integrity of microtubules possibly by influencing their stability. Involved in an anchoring mechanism to maintain tea2 and tip1 at growing microtubule ends. Strongly stimulates the ATPase activity of tea2. Publication Abstract from PubMed Using cryo-electron microscopy, we characterize the architecture of microtubules assembled from Schizosaccharomyces pombe tubulin, in the presence and absence of their regulatory partner Mal3. Cryo-electron tomography reveals that microtubules assembled from S. pombe tubulin have predominantly B-lattice interprotofilament contacts, with protofilaments skewed around the microtubule axis. Copolymerization with Mal3 favors 13 protofilament microtubules with reduced protofilament skew, indicating that Mal3 adjusts interprotofilament interfaces. A 4.6-A resolution structure of microtubule-bound Mal3 shows that Mal3 makes a distinctive footprint on the S. pombe microtubule lattice and that unlike mammalian microtubules, S. pombe microtubules do not show the longitudinal lattice compaction associated with EB protein binding and GTP hydrolysis. Our results firmly support a structural plasticity view of microtubule dynamics in which microtubule lattice conformation is sensitive to a variety of effectors and differently so for different tubulins. Nucleotide- and Mal3-dependent changes in fission yeast microtubules suggest a structural plasticity view of dynamics.,von Loeffelholz O, Venables NA, Drummond DR, Katsuki M, Cross R, Moores CA Nat Commun. 2017 Dec 13;8(1):2110. doi: 10.1038/s41467-017-02241-5. PMID:29235477 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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