- EMDB-28999: Engineered human dynein motor domain in microtubule-bound state -
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基本情報
登録情報
データベース: EMDB / ID: EMD-28999
タイトル
Engineered human dynein motor domain in microtubule-bound state
マップデータ
Sharpened map of human dynein motor domain in microtubule-bound mutant (dynein MT-B)
試料
複合体: Engineered human dynein motor domain in microtubule-bound state
タンパク質・ペプチド: Cytoplasmic dynein 1 heavy chain 1,Serine--tRNA ligase
リガンド: ADENOSINE-5'-DIPHOSPHATE
リガンド: ADENOSINE-5'-TRIPHOSPHATE
キーワード
Dynein / motor domain / microtubule-bound / MOTOR PROTEIN
機能・相同性
機能・相同性情報
selenocysteine biosynthetic process / seryl-tRNA aminoacylation / serine-tRNA ligase / serine-tRNA ligase activity / positive regulation of intracellular transport / regulation of metaphase plate congression / establishment of spindle localization / positive regulation of spindle assembly / dynein complex / COPI-independent Golgi-to-ER retrograde traffic ...selenocysteine biosynthetic process / seryl-tRNA aminoacylation / serine-tRNA ligase / serine-tRNA ligase activity / positive regulation of intracellular transport / regulation of metaphase plate congression / establishment of spindle localization / positive regulation of spindle assembly / dynein complex / COPI-independent Golgi-to-ER retrograde traffic / minus-end-directed microtubule motor activity / retrograde axonal transport / dynein light intermediate chain binding / cytoplasmic dynein complex / P-body assembly / nuclear migration / dynein intermediate chain binding / cytoplasmic microtubule / Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / COPI-mediated anterograde transport / cytoplasmic microtubule organization / stress granule assembly / Mitotic Prometaphase / EML4 and NUDC in mitotic spindle formation / regulation of mitotic spindle organization / Loss of Nlp from mitotic centrosomes / Loss of proteins required for interphase microtubule organization from the centrosome / Recruitment of mitotic centrosome proteins and complexes / axon cytoplasm / Recruitment of NuMA to mitotic centrosomes / Anchoring of the basal body to the plasma membrane / Resolution of Sister Chromatid Cohesion / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / MHC class II antigen presentation / AURKA Activation by TPX2 / mitotic spindle organization / filopodium / RHO GTPases Activate Formins / Aggrephagy / HCMV Early Events / Separation of Sister Chromatids / azurophil granule lumen / Regulation of PLK1 Activity at G2/M Transition / positive regulation of cold-induced thermogenesis / cell cortex / microtubule / cell division / centrosome / Neutrophil degranulation / ATP hydrolysis activity / RNA binding / extracellular exosome / extracellular region / ATP binding / membrane / cytosol / cytoplasm 類似検索 - 分子機能
Serine-tRNA synthetase, type1, N-terminal / Seryl-tRNA synthetase N-terminal domain / Serine-tRNA ligase, type1 / Serine-tRNA ligase catalytic core domain / Serine-tRNA synthetase, type1, N-terminal domain superfamily / Dynein heavy chain, AAA 5 extension domain / Dynein heavy chain AAA lid domain / Class I and II aminoacyl-tRNA synthetase, tRNA-binding arm / Dynein heavy chain, C-terminal domain / Dynein heavy chain, C-terminal domain, barrel region ...Serine-tRNA synthetase, type1, N-terminal / Seryl-tRNA synthetase N-terminal domain / Serine-tRNA ligase, type1 / Serine-tRNA ligase catalytic core domain / Serine-tRNA synthetase, type1, N-terminal domain superfamily / Dynein heavy chain, AAA 5 extension domain / Dynein heavy chain AAA lid domain / Class I and II aminoacyl-tRNA synthetase, tRNA-binding arm / Dynein heavy chain, C-terminal domain / Dynein heavy chain, C-terminal domain, barrel region / Dynein heavy chain C-terminal domain / P-loop containing dynein motor region / Dynein heavy chain, tail / Dynein heavy chain, N-terminal region 1 / Dynein heavy chain / Dynein heavy chain region D6 P-loop domain / Dynein heavy chain, linker / Dynein heavy chain, AAA module D4 / Dynein heavy chain, coiled coil stalk / Dynein heavy chain, hydrolytic ATP-binding dynein motor region / Dynein heavy chain, ATP-binding dynein motor region / Dynein heavy chain AAA lid domain / Dynein heavy chain AAA lid domain superfamily / Dynein heavy chain, domain 2, N-terminal / Dynein heavy chain, linker, subdomain 3 / Dynein heavy chain, AAA1 domain, small subdomain / Dynein heavy chain region D6 P-loop domain / Dynein heavy chain, N-terminal region 2 / Hydrolytic ATP binding site of dynein motor region / Microtubule-binding stalk of dynein motor / P-loop containing dynein motor region D4 / ATP-binding dynein motor region / Dynein heavy chain AAA lid domain / Aminoacyl-tRNA synthetase, class II (G/ P/ S/T) / tRNA synthetase class II core domain (G, H, P, S and T) / Aminoacyl-tRNA synthetase, class II / Aminoacyl-transfer RNA synthetases class-II family profile. / Class II Aminoacyl-tRNA synthetase/Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL) / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / P-loop containing nucleoside triphosphate hydrolase 類似検索 - ドメイン・相同性
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
R35GM139483
米国
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
R35GM142959
米国
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
S10OD023603
米国
引用
ジャーナル: Nat Struct Mol Biol / 年: 2023 タイトル: Microtubule-binding-induced allostery triggers LIS1 dissociation from dynein prior to cargo transport. 著者: William D Ton / Yue Wang / Pengxin Chai / Cisloynny Beauchamp-Perez / Nicholas T Flint / Lindsay G Lammers / Hao Xiong / Kai Zhang / Steven M Markus / 要旨: The lissencephaly-related protein LIS1 is a critical regulator of cytoplasmic dynein that governs motor function and intracellular localization (for example, to microtubule plus-ends). Although LIS1 ...The lissencephaly-related protein LIS1 is a critical regulator of cytoplasmic dynein that governs motor function and intracellular localization (for example, to microtubule plus-ends). Although LIS1 binding is required for dynein activity, its unbinding prior to initiation of cargo transport is equally important, since preventing dissociation leads to dynein dysfunction. To understand whether and how dynein-LIS1 binding is modulated, we engineered dynein mutants locked in a microtubule-bound (MT-B) or microtubule-unbound (MT-U) state. Whereas the MT-B mutant exhibits low LIS1 affinity, the MT-U mutant binds LIS1 with high affinity, and as a consequence remains almost irreversibly associated with microtubule plus-ends. We find that a monomeric motor domain is sufficient to exhibit these opposing LIS1 affinities, and that this is evolutionarily conserved between yeast and humans. Three cryo-EM structures of human dynein with and without LIS1 reveal microtubule-binding induced conformational changes responsible for this regulation. Our work reveals key biochemical and structural insight into LIS1-mediated dynein activation.
全体 : Engineered human dynein motor domain in microtubule-bound state
全体
名称: Engineered human dynein motor domain in microtubule-bound state
要素
複合体: Engineered human dynein motor domain in microtubule-bound state
タンパク質・ペプチド: Cytoplasmic dynein 1 heavy chain 1,Serine--tRNA ligase
リガンド: ADENOSINE-5'-DIPHOSPHATE
リガンド: ADENOSINE-5'-TRIPHOSPHATE
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超分子 #1: Engineered human dynein motor domain in microtubule-bound state
超分子
名称: Engineered human dynein motor domain in microtubule-bound state タイプ: complex / ID: 1 / 親要素: 0 / 含まれる分子: #1
由来(天然)
生物種: Homo sapiens (ヒト)
分子量
理論値: 350 KDa
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分子 #1: Cytoplasmic dynein 1 heavy chain 1,Serine--tRNA ligase
分子
名称: Cytoplasmic dynein 1 heavy chain 1,Serine--tRNA ligase タイプ: protein_or_peptide / ID: 1 詳細: residues 1458-3281 of dynein followed by residues 30-96 of serine-tRNA ligase, followed by residues 3412-4646 of dynein コピー数: 1 / 光学異性体: LEVO / EC番号: serine-tRNA ligase