4abo

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

Loading... Status: waiting for Mol* initialization 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. Method: Electron Microscopy, Resolution 8.6Å Ligands: GSP, GTP 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 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.

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