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-Structure paper
タイトル | Template-free 13-protofilament microtubule-MAP assembly visualized at 8 A resolution. |
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ジャーナル・号・ページ | J Cell Biol, Vol. 191, Issue 3, Page 463-470, Year 2010 |
掲載日 | 2010年11月1日 |
著者 | Franck J Fourniol / Charles V Sindelar / Béatrice Amigues / Daniel K Clare / Geraint Thomas / Mylène Perderiset / Fiona Francis / Anne Houdusse / Carolyn A Moores / |
PubMed 要旨 | 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. |
リンク | J Cell Biol / PubMed:20974813 / PubMed Central |
手法 | EM (単粒子) / EM (らせん対称) |
解像度 | 8.2 - 13.5 Å |
構造データ | EMDB-1787: |
化合物 | ChemComp-GDP: ChemComp-GTP: |
由来 |
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キーワード | STRUCTURAL PROTEIN |