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Title | Template-free 13-protofilament microtubule-MAP assembly visualized at 8 A resolution. |
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Journal, issue, pages | J Cell Biol, Vol. 191, Issue 3, Page 463-470, Year 2010 |
Publish date | Nov 1, 2010 |
Authors | Franck J Fourniol / Charles V Sindelar / Béatrice Amigues / Daniel K Clare / Geraint Thomas / Mylène Perderiset / Fiona Francis / Anne Houdusse / Carolyn A Moores / |
PubMed Abstract | Microtubule-associated proteins (MAPs) are essential for regulating and organizing cellular microtubules (MTs). However, our mechanistic understanding of MAP function is limited by a lack of detailed ...Microtubule-associated proteins (MAPs) are essential for regulating and organizing cellular microtubules (MTs). However, our mechanistic understanding of MAP function is limited by a lack of detailed structural information. Using cryo-electron microscopy and single particle algorithms, we solved the 8 Å structure of doublecortin (DCX)-stabilized MTs. Because of DCX's unusual ability to specifically nucleate and stabilize 13-protofilament MTs, our reconstruction provides unprecedented insight into the structure of MTs with an in vivo architecture, and in the absence of a stabilizing drug. DCX specifically recognizes the corner of four tubulin dimers, a binding mode ideally suited to stabilizing both lateral and longitudinal lattice contacts. A striking consequence of this is that DCX does not bind the MT seam. DCX binding on the MT surface indirectly stabilizes conserved tubulin-tubulin lateral contacts in the MT lumen, operating independently of the nucleotide bound to tubulin. DCX's exquisite binding selectivity uncovers important insights into regulation of cellular MTs. |
External links | J Cell Biol / PubMed:20974813 / PubMed Central |
Methods | EM (single particle) / EM (helical sym.) |
Resolution | 8.2 - 13.5 Å |
Structure data | EMDB-1787: |
Chemicals | ChemComp-GDP: ChemComp-GTP: |
Source |
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Keywords | STRUCTURAL PROTEIN |