EMDB/PDB/SASBDBから引用されている文献のデータベース

キーワード
構造解析手法	All X線回折 NMR 電子顕微鏡小角散乱中性子線回折線維回折粉末回折赤外分光 EPR FRET 理論モデルハイブリッド
著者・登録者
ジャーナル
IF	>30 >20 >10 >5 all

タイトル	Cryo-EM structures of the tubulin cofactors reveal the molecular basis of alpha/beta-tubulin biogenesis.
ジャーナル・号・ページ	Nat Commun, Year 2025
掲載日	2025年12月29日
著者	Aryan Taheri / Zhoaqian Wang / Bharti Singal / Fei Guo / Jawdat Al-Bassam /
PubMed 要旨	Microtubule polarity and dynamic polymerization arise from the self-association properties of the αβ-tubulin heterodimer. For decades, it has remained unclear how the tubulin cofactors TBCD, TBCE, ...Microtubule polarity and dynamic polymerization arise from the self-association properties of the αβ-tubulin heterodimer. For decades, it has remained unclear how the tubulin cofactors TBCD, TBCE, TBCC, and the Arl2 GTPase mediate the biogenesis of αβ-tubulin from individual α- and β-tubulins. Here, we use cryo-electron microscopy to determine structures of tubulin cofactors bound to αβ-tubulin. TBCD, TBCE, and Arl2 form a heterotrimeric cage-like assembly, we term TBC-DEG, around the αβ-tubulin heterodimer. The TBC-DEG-αβ-tubulin structures show that TBC-DEG wraps around β-tubulin while TBCE extends along α-tubulin. The TBC-DEG/TBCC-αβ-tubulin structures reveal that TBCC forms multi-domain interactions with Arl2 and TBCD to engage the αβ-tubulin intradimer-interface, promoting TBCE rotation while TBCD holds β-tubulin. TBCC engages the GTP-bound Arl2, multiple sites of TBCD, and the native αβ-tubulin intradimer interface near the α-tubulin N-site GTP. Together, these structures uncover transition states for αβ-tubulin biogenesis and degradation, suggesting a vise-like, GTP-hydrolysis-dependent mechanism in which TBCC binding to TBC-DEG modulates αβ-tubulin interfaces. Our studies provide structural evidence that tubulin cofactors act as enzymatic regulators that assemble the invariant αβ-tubulin architecture. By catalyzing α- and β-tubulin biogenesis and degradation, the TBC-DEG and TBCC assemblies regulate the polymerization competency of αβ-tubulin for microtubule formation.
リンク	Nat Commun / PubMed:41461644
手法	EM (単粒子)
解像度	3.49 - 3.89 Å
構造データ	47947 9edr EMDB-47947, PDB-9edr: Tubulin Cofactors D,E,G,C and Tubulin complex -- TBCC N Terminus Bound to Tubulin 手法: EM (単粒子) / 解像度: 3.8 Å 47948 9eds EMDB-47948, PDB-9eds: Tubulin cofactors D,E,G,C bound to tubulin dimer -- TBCC N terminus unbound 手法: EM (単粒子) / 解像度: 3.8 Å 47949 9edt EMDB-47949, PDB-9edt: Tubulin cofactors D,E,G bound to tubulin dimer 手法: EM (単粒子) / 解像度: 3.7 Å 47954 9eeb EMDB-47954, PDB-9eeb: Tubulin cofactors D,E,G bound to tubulin dimer 手法: EM (単粒子) / 解像度: 3.7 Å EMDB-70497: Tubulin cofactors D, Arl2, tubulin dimer 手法: EM (単粒子) / 解像度: 3.62 Å EMDB-70498: Tubulin cofactors D,E,G bound to tubulin dimer. Class 2 手法: EM (単粒子) / 解像度: 3.82 Å EMDB-70499: Tubulin cofactors D,E,G bound to tubulin dimer. Class 1 手法: EM (単粒子) / 解像度: 3.89 Å EMDB-70504: Tubulin Cofactors D,E,G,C and Tubulin complex -- TBCC N Terminus Bound to Tubulin Core Refinement 手法: EM (単粒子) / 解像度: 3.73 Å EMDB-70505: Tubulin Cofactors D,E,G,C and Tubulin complex -- TBCC N Terminus Bound to Tubulin. TBCC Focused 手法: EM (単粒子) / 解像度: 3.75 Å EMDB-70506: Tubulin Cofactors D,E,G,C and Tubulin complex -- TBCC N Terminus Bound to Tubulin. TBC E Refinement 手法: EM (単粒子) / 解像度: 3.61 Å EMDB-70516: Tubulin cofactors D,E,G,C bound to tubulin dimer -- TBCC N terminus unbound. Core Refinement 手法: EM (単粒子) / 解像度: 3.83 Å EMDB-70518: Tubulin cofactors D,E,G,C bound to tubulin dimer -- TBCC N terminus unbound. TBCE Refinement 手法: EM (単粒子) / 解像度: 3.49 Å
化合物	ChemComp-GTP: GUANOSINE-5'-TRIPHOSPHATE / GTP / GTP, エネルギー貯蔵分子YM ChemComp-GDP: GUANOSINE-5'-DIPHOSPHATE / GDP / GDP, エネルギー貯蔵分子YM
由来	saccharomyces cerevisiae (パン酵母) sus scrofa (ブタ) escherichia coli (大腸菌)
キーワード	CYTOSOLIC PROTEIN / Cytoskeleton / tubulin / tubulin cofactors / microtubules / tubulin biogenesis / tubulin degredation / Cofactors / Tubulin biogeneis / Tubulin degradation