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	Kinesin-8-specific loop-2 controls the dual activities of the motor domain according to tubulin protofilament shape.
ジャーナル・号・ページ	Nat Commun, Vol. 13, Issue 1, Page 4198, Year 2022
掲載日	2022年7月20日
著者	Byron Hunter / Matthieu P M H Benoit / Ana B Asenjo / Caitlin Doubleday / Daria Trofimova / Corey Frazer / Irsa Shoukat / Hernando Sosa / John S Allingham /
PubMed 要旨	Kinesin-8s are dual-activity motor proteins that can move processively on microtubules and depolymerize microtubule plus-ends, but their mechanism of combining these distinct activities remains ...Kinesin-8s are dual-activity motor proteins that can move processively on microtubules and depolymerize microtubule plus-ends, but their mechanism of combining these distinct activities remains unclear. We addressed this by obtaining cryo-EM structures (2.6-3.9 Å) of Candida albicans Kip3 in different catalytic states on the microtubule lattice and on a curved microtubule end mimic. We also determined a crystal structure of microtubule-unbound CaKip3-ADP (2.0 Å) and analyzed the biochemical activity of CaKip3 and kinesin-1 mutants. These data reveal that the microtubule depolymerization activity of kinesin-8 originates from conformational changes of its motor core that are amplified by dynamic contacts between its extended loop-2 and tubulin. On curved microtubule ends, loop-1 inserts into preceding motor domains, forming head-to-tail arrays of kinesin-8s that complement loop-2 contacts with curved tubulin and assist depolymerization. On straight tubulin protofilaments in the microtubule lattice, loop-2-tubulin contacts inhibit conformational changes in the motor core, but in the ADP-Pi state these contacts are relaxed, allowing neck-linker docking for motility. We propose that these tubulin shape-induced alternations between pro-microtubule-depolymerization and pro-motility kinesin states, regulated by loop-2, are the key to the dual activity of kinesin-8 motors.
リンク	Nat Commun / PubMed:35859148 / PubMed Central
手法	EM (らせん対称) / EM (単粒子) / X線回折
解像度	2.01 - 3.9 Å
構造データ	26074 7tqx EMDB-26074, PDB-7tqx: CaKip3[2-482] - AMP-PNP in complex with a microtubule 手法: EM (らせん対称) / 解像度: 2.8 Å 26075 7tqy EMDB-26075, PDB-7tqy: CaKip3[2-482] - ADP-AlFx in complex with a microtubule 手法: EM (らせん対称) / 解像度: 2.6 Å 26076 7tqz EMDB-26076, PDB-7tqz: Apo CaKip3[2-482] in complex with a microtubule 手法: EM (らせん対称) / 解像度: 2.7 Å 26077 7tr0 EMDB-26077, PDB-7tr0: CaKip3[2-436] - AMP-PNP in complex with a microtubule 手法: EM (らせん対称) / 解像度: 2.7 Å 26078 7tr1 EMDB-26078, PDB-7tr1: CaKip3[2-436]-L2-mutant(HsKHC) - AMP-PNP in complex with a microtubule 手法: EM (らせん対称) / 解像度: 3.1 Å 26079 7tr2 EMDB-26079, PDB-7tr2: Apo CaKip3[2-436]-L2-mutant(HsKHC) in complex with a microtubule 手法: EM (らせん対称) / 解像度: 3.0 Å 26080 7tr3 EMDB-26080, PDB-7tr3: CaKip3[2-482] - AMP-PNP in complex with a dolastatin-10-stabilized tubulin ring 手法: EM (単粒子) / 解像度: 3.9 Å PDB-7lff: Crystal structure of the Candida albicans kinesin-8 motor domain 手法: X-RAY DIFFRACTION / 解像度: 2.01 Å
化合物	ChemComp-ADP: ADENOSINE-5'-DIPHOSPHATE / ADP / ADP, エネルギー貯蔵分子YM / アデノシン二リン酸 ChemComp-MG: Unknown entry / マグネシウムジカチオン ChemComp-HOH: WATER / 水 ChemComp-GTP: GUANOSINE-5'-TRIPHOSPHATE / GTP / GTP, エネルギー貯蔵分子YM / グアノシン三リン酸 ChemComp-GDP: GUANOSINE-5'-DIPHOSPHATE / GDP / GDP, エネルギー貯蔵分子YM / グアノシン二リン酸 ChemComp-TA1: TAXOL / パクリタキセル / 薬剤, 化学療法薬YM / パクリタキセル ChemComp-ANP: PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / AMP-PNP / AMP-PNP, エネルギー貯蔵分子類似体YM ChemComp-AF3: ALUMINUM FLUORIDE / トリフルオロアルミニウム / フッ化アルミニウム ChemComp-SR6*: dolastatin-10 / ドラスタチン10
由来	candida albicans (酵母) sus scrofa (ブタ) candida albicans (strain sc5314 / atcc mya-2876) (酵母) homo sapiens (ヒト)
キーワード	MOTOR PROTEIN (モータータンパク質) / kinesin (キネシン) / microtubule (微小管) / depolymerase / motility (運動性) / cytoskeleton (細胞骨格) / Kip3 / tubulin (チューブリン) / dolastatin-10