PDB-7kzm: Outer dynein arm bound to doublet microtubules from C. reinhardtii

基本情報

• 登録情報: データベース: PDB / ID: 7kzm
• タイトル: Outer dynein arm bound to doublet microtubules from C. reinhardtii

要素

• (Dynein light chain ...) x 4
• (Flagellar outer dynein arm ...) x 2
• (Outer dynein arm-docking complex ...) x 2
• DC1
• DC2
• Dynein 11 kDa light chain, flagellar outer arm
• Dynein 18 kDa light chain, flagellar outer arm
• Dynein 8 kDa light chain, flagellar outer arm
• Dynein gamma chain, flagellar outer arm
• Dynein, 70 kDa intermediate chain, flagellar outer arm
• Dynein, 78 kDa intermediate chain, flagellar outer arm
• Heavy chain alpha
• Outer dynein arm protein 1
• Tubulin alpha
• Tubulin beta

• キーワード: MOTOR PROTEIN / dynein / microtubule / cilia

機能・相同性

分子機能:

outer dynein arm / outer dynein arm assembly / cilium movement involved in cell motility / 9+2 motile cilium / dynein light chain binding / cilium movement / motile cilium assembly / dynein heavy chain binding / axonemal dynein complex / dynein complex / cell projection organization / minus-end-directed microtubule motor activity / dynein light intermediate chain binding / cytoplasmic dynein complex / ciliary plasm / motile cilium / dynein intermediate chain binding / microtubule-based movement / axoneme / microtubule-based process / enzyme regulator activity / 加水分解酵素; 酸無水物に作用; GTPに作用・細胞または細胞小器官の運動に関与 / structural constituent of cytoskeleton / microtubule cytoskeleton organization / mitotic cell cycle / microtubule / hydrolase activity / GTPase activity / calcium ion binding / GTP binding / ATP hydrolysis activity / ATP binding / metal ion binding / cytoplasm

ドメイン・相同性:

: / ODAD1 central coiled coil region / Kelch repeat type 2 / Kelch motif / Dynein light chain roadblock-type 1/2 / Galactose oxidase, central domain / Dynein light chain Tctex-1 like / Tctex-1-like superfamily / Tctex-1 family / Phospholipase D/Transphosphatidylase / Phospholipase D phosphodiesterase active site profile. / Dynein light chain, type 1/2, conserved site / Dynein light chain type 1 signature. / Dynein light chain type 1 / Dynein light chain, type 1/2 / Dynein light chain superfamily / Dynein light chain type 1 / Dynein heavy chain, AAA 5 extension domain / Dynein heavy chain AAA lid domain / Roadblock/LAMTOR2 domain / Roadblock/LC7 domain / Roadblock/LC7 domain / Dynein heavy chain 3, AAA+ lid domain / AAA+ lid domain / Filamin/ABP280 repeat / Filamin-type immunoglobulin domains / Dynein heavy chain, C-terminal domain / Dynein heavy chain, C-terminal domain, barrel region / Dynein heavy chain C-terminal domain / Galactose oxidase/kelch, beta-propeller / Filamin/ABP280 repeat / Filamin/ABP280 repeat profile. / Filamin/ABP280 repeat-like / 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 / IPT/TIG domain / Kelch-type beta propeller / IPT domain / Tubulin-beta mRNA autoregulation signal. / Alpha tubulin / Beta tubulin, autoregulation binding site / Beta tubulin / Tubulin / Tubulin, C-terminal / Tubulin C-terminal domain / Tubulin, conserved site / Tubulin subunits alpha, beta, and gamma signature. / Tubulin/FtsZ family, C-terminal domain / Tubulin/FtsZ-like, C-terminal domain / Tubulin/FtsZ, C-terminal / Tubulin/FtsZ, 2-layer sandwich domain / Tubulin/FtsZ family, GTPase domain / Tubulin/FtsZ family, GTPase domain / Tubulin/FtsZ, GTPase domain / Tubulin/FtsZ, GTPase domain superfamily / EF-hand domain pair / EF-hand, calcium binding motif / EF-Hand 1, calcium-binding site / EF-hand calcium-binding domain. / EF-hand calcium-binding domain profile. / EF-hand domain / EF-hand domain pair / Immunoglobulin E-set / Trp-Asp (WD) repeats circular profile. / WD domain, G-beta repeat / WD40 repeats / WD40 repeat / WD40-repeat-containing domain superfamily / WD40/YVTN repeat-like-containing domain superfamily / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / Immunoglobulin-like fold / P-loop containing nucleoside triphosphate hydrolase

構成要素:

GUANOSINE-5'-DIPHOSPHATE / GUANOSINE-5'-TRIPHOSPHATE / PLD phosphodiesterase domain-containing protein / Uncharacterized protein / Dynein light chain roadblock / Uncharacterized protein / Dynein light chain / Outer dynein arm protein 1 / Mr19,000 outer arm dynein light chain / Tubulin beta-1/beta-2 chain / Tubulin alpha-1 chain / Dynein, 70 kDa intermediate chain, flagellar outer arm / Dynein light chain 9 / Dynein gamma chain, flagellar outer arm / Dynein, 78 kDa intermediate chain, flagellar outer arm / Dynein 11 kDa light chain, flagellar outer arm / Dynein 8 kDa light chain, flagellar outer arm / Dynein 18 kDa light chain, flagellar outer arm / Outer dynein arm-docking complex protein DC3 / Dynein light chain roadblock

• 生物種: Chlamydomonas reinhardtii (クラミドモナス)
• 手法: 電子顕微鏡法 / らせん対称体再構成法 / クライオ電子顕微鏡法 / 解像度: 7.5 Å
• データ登録者: Walton, T. / Wu, H. / Brown, A.B.
• 引用: ジャーナル: Nat Commun / 年: 2021; タイトル: Structure of a microtubule-bound axonemal dynein.; 著者: Travis Walton / Hao Wu / Alan Brown / ; 要旨: Axonemal dyneins are tethered to doublet microtubules inside cilia to drive ciliary beating, a process critical for cellular motility and extracellular fluid flow. Axonemal dyneins are evolutionarily and biochemically distinct from cytoplasmic dyneins that transport cargo, and the mechanisms regulating their localization and function are poorly understood. Here, we report a single-particle cryo-EM reconstruction of a three-headed axonemal dynein natively bound to doublet microtubules isolated from cilia. The slanted conformation of the axonemal dynein causes interaction of its motor domains with the neighboring dynein complex. Our structure shows how a heterotrimeric docking complex specifically localizes the linear array of axonemal dyneins to the doublet microtubule by directly interacting with the heavy chains. Our structural analysis establishes the arrangement of conserved heavy, intermediate and light chain subunits, and provides a framework to understand the roles of individual subunits and the interactions between dyneins during ciliary waveform generation.

履歴

登録	2020年12月10日	登録サイト: RCSB / 処理サイト: RCSB
改定 1.0	2021年1月20日	Provider: repository / タイプ: Initial release
改定 1.1	2021年2月3日	Group: Database references / カテゴリ: citation / citation_author Item: _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_PubMed / _citation.title / _citation_author.identifier_ORCID / _citation_author.name
改定 1.2	2024年3月6日	Group: Data collection / Database references / カテゴリ: chem_comp_atom / chem_comp_bond / database_2 Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession