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4ABO

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

Summary for 4ABO
Entry DOI10.2210/pdb4abo/pdb
Related1FFX 1IA0 1JFF 1TUB
EMDB information2004 2005 2006
DescriptorTUBULIN BETA CHAIN, TUBULIN ALPHA-1A CHAIN, MICROTUBULE INTEGRITY PROTEIN MAL3, ... (5 entities in total)
Functional Keywordsstructural protein, cytoskeleton, gtpase, end binding
Biological sourceSCHIZOSACCHAROMYCES POMBE (FISSION YEAST)
More
Cellular locationCytoplasm, cytoskeleton : Q10113
Total number of polymer chains9
Total formula weight421064.68
Authors
Maurer, S.P.,Fourniol, F.J.,Bohner, G.,Moores, C.A.,Surrey, T. (deposition date: 2011-12-09, release date: 2012-06-06, Last modification date: 2024-05-08)
Primary citationMaurer, S.P.,Fourniol, F.J.,Bohner, G.,Moores, C.A.,Surrey, T.
Ebs Recognize a Nucleotide-Dependent Structural CAP at Growing Microtubule Ends.
Cell(Cambridge,Mass.), 149:371-, 2012
Cited by
PubMed Abstract: 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.
PubMed: 22500803
DOI: 10.1016/J.CELL.2012.02.049
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (8.6 Å)
Structure validation

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