4abo | pdb_00004abo

Mal3 CH domain homology model and mammalian tubulin (2XRP) docked into the 8.6-Angstrom cryo-EM map of Mal3-GTPgammaS-microtubules

spinqualitylabelsall models 4abo, resolution 8.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4abo is a 9 chain structure with sequence from Schizosaccharomyces pombe and Sus scrofa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GSP, GTP Related: 1tub, 1ffx, 1ia0, 1jff Activity: Tubulin GTPase, with EC number 3.6.5.6 Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed Growing microtubule ends serve as transient binding platforms for essential proteins that regulate microtubule dynamics and their interactions with cellular substructures. End-binding proteins (EBs) autonomously recognize an extended region at growing microtubule ends with unknown structural characteristics and then recruit other factors to the dynamic end structure. Using cryo-electron microscopy, subnanometer single-particle reconstruction, and fluorescence imaging, we present a pseudoatomic model of how the calponin homology (CH) domain of the fission yeast EB Mal3 binds to the end regions of growing microtubules. The Mal3 CH domain bridges protofilaments except at the microtubule seam. By binding close to the exchangeable GTP-binding site, the CH domain is ideally positioned to sense the microtubule's nucleotide state. The same microtubule-end region is also a stabilizing structural cap protecting the microtubule from depolymerization. This insight supports a common structural link between two important biological phenomena, microtubule dynamic instability and end tracking. EBs recognize a nucleotide-dependent structural cap at growing microtubule ends.,Maurer SP, Fourniol FJ, Bohner G, Moores CA, Surrey T Cell. 2012 Apr 13;149(2):371-82. PMID:22500803 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Tubulin

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