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- EMDB-14151: BtubA(R284G,K286D,F287G):BtubB bacterial tubulin M-loop mutant fo... -
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Open data
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Basic information
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Title | BtubA(R284G,K286D,F287G):BtubB bacterial tubulin M-loop mutant forming a single protofilament (Prosthecobacter dejongeii) | |||||||||
![]() | BtubA(R284G,K286D,F287G):BtubB bacterial tubulin M-loop mutant forming a single protofilament | |||||||||
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![]() | Cytyoskeleton / tubulin-like / cytomotive filaments / CELL CYCLE | |||||||||
Function / homology | ![]() microtubule-based process / structural constituent of cytoskeleton / microtubule / GTP binding Similarity search - Function | |||||||||
Biological species | ![]() ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.6 Å | |||||||||
![]() | Wagstaff J / Planelles-Herrero VJ | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Diverse cytomotive actins and tubulins share a polymerization switch mechanism conferring robust dynamics. Authors: James Mark Wagstaff / Vicente José Planelles-Herrero / Grigory Sharov / Aisha Alnami / Frank Kozielski / Emmanuel Derivery / Jan Löwe / ![]() Abstract: Protein filaments are used in myriads of ways to organize other molecules within cells. Some filament-forming proteins couple the hydrolysis of nucleotides to their polymerization cycle, thus ...Protein filaments are used in myriads of ways to organize other molecules within cells. Some filament-forming proteins couple the hydrolysis of nucleotides to their polymerization cycle, thus powering the movement of other molecules. These filaments are termed cytomotive. Only members of the actin and tubulin protein superfamilies are known to form cytomotive filaments. We examined the basis of cytomotivity via structural studies of the polymerization cycles of actin and tubulin homologs from across the tree of life. We analyzed published data and performed structural experiments designed to disentangle functional components of these complex filament systems. Our analysis demonstrates the existence of shared subunit polymerization switches among both cytomotive actins and tubulins, i.e., the conformation of subunits switches upon assembly into filaments. These cytomotive switches can explain filament robustness, by enabling the coupling of kinetic and structural polarities required for cytomotive behaviors and by ensuring that single cytomotive filaments do not fall apart. | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 226.8 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 13.5 KB 13.5 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 14.1 KB | Display | ![]() |
Images | ![]() | 81.3 KB | ||
Filedesc metadata | ![]() | 6 KB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 649.1 KB | Display | ![]() |
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Full document | ![]() | 648.7 KB | Display | |
Data in XML | ![]() | 14 KB | Display | |
Data in CIF | ![]() | 19 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 7quqMC ![]() 7qucC ![]() 7qudC ![]() 7qupC M: atomic model generated by this map C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Annotation | BtubA(R284G,K286D,F287G):BtubB bacterial tubulin M-loop mutant forming a single protofilament | ||||||||||||||||||||
Voxel size | X=Y=Z: 1.055 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
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Sample components
-Entire : BtubAB heterodimer
Entire | Name: BtubAB heterodimer |
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Components |
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-Supramolecule #1: BtubAB heterodimer
Supramolecule | Name: BtubAB heterodimer / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2 / Details: M-loop mutant BtubA(R284G,K286D,F287G) |
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Source (natural) | Organism: ![]() ![]() |
-Macromolecule #1: Tubulin domain-containing protein
Macromolecule | Name: Tubulin domain-containing protein / type: protein_or_peptide / ID: 1 / Number of copies: 3 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 51.095012 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MKVNNTIVVS IGQAGNQIAA SFWKTVCLEH GIDPLTGQTA PGVAPRGNWS SFFSKLGESS SGSYVPRAIM VDLEPSVIDN VKATSGSLF NPANLISRTE GAGGNFAVGY LGAGREVLPE VMSRLDYEID KCDNVGGIIV LHAIGGGTGS GFGALLIESL K EKYGEIPV ...String: MKVNNTIVVS IGQAGNQIAA SFWKTVCLEH GIDPLTGQTA PGVAPRGNWS SFFSKLGESS SGSYVPRAIM VDLEPSVIDN VKATSGSLF NPANLISRTE GAGGNFAVGY LGAGREVLPE VMSRLDYEID KCDNVGGIIV LHAIGGGTGS GFGALLIESL K EKYGEIPV LSCAVLPSPQ VSSVVTEPYN TVFALNTLRR SADACLIFDN EALFDLAHRK WNIESPTVDD LNLLITEALA GI TASMRFS GFLTVEISLR ELLTNLVPQP SLHFLMCAFA PLTPPDGSDG EELGIEEMIK SLFDNGSVFA ACSPMEGRFL STA VLYRGI MEDKPLADAA LAAMREKLPL TYWIPTAFKI GYVEQPGISH RKSMVLLANN TEIARVLDRI CHNFDKLWQR KAFA NWYLN EGMSEEQINV LRASAQELVQ SYQVAEESGA KAKVQDSAGD TGMRAAAAGV SDDARGSMSL RDLVDRRR UniProtKB: Tubulin domain-containing protein |
-Macromolecule #2: Tubulin beta
Macromolecule | Name: Tubulin beta / type: protein_or_peptide / ID: 2 / Number of copies: 3 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 46.49757 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MREILSIHVG QCGNQIADSF WRLALREHGL TEAGTLKEGS NAAANSNMEV FFHKVRDGKY VPRAVLVDLE PGVIARIEGG DMSQLFDES SIVRKIPGAA NNWARGYNVE GEKVIDQIMN VIDSAVEKTK GLQGFLMTHS IGGGSGSGLG SLILERLRQA Y PKKRIFTF ...String: MREILSIHVG QCGNQIADSF WRLALREHGL TEAGTLKEGS NAAANSNMEV FFHKVRDGKY VPRAVLVDLE PGVIARIEGG DMSQLFDES SIVRKIPGAA NNWARGYNVE GEKVIDQIMN VIDSAVEKTK GLQGFLMTHS IGGGSGSGLG SLILERLRQA Y PKKRIFTF SVVPSPLISD SAVEPYNAIL TLQRILDNAD GAVLLDNEAL FRIAKAKLNR SPNYMDLNNI IALIVSSVTA SL RFPGKLN TDLSEFVTNL VPFPGNHFLT ASFAPMRGAG QEGQVRTNFP DLARETFAQD NFTAAIDWQQ GVYLAASALF RGD VKAKDV DENMATIRKS LNYASYMPAS GGLKLGYAET APEGFASSGL ALVNHTGIAA VFERLIAQFD IMFDNHAYTH WYEN AGVSR DMMAKARNQI ATLAQSYRDA S UniProtKB: Tubulin beta |
-Macromolecule #3: PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER
Macromolecule | Name: PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER / type: ligand / ID: 3 / Number of copies: 6 / Formula: G2P |
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Molecular weight | Theoretical: 521.208 Da |
Chemical component information | ![]() ChemComp-G2P: |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 7.7 |
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Grid | Model: UltrAuFoil R1.2/1.3 / Material: GOLD |
Vitrification | Cryogen name: NITROGEN |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Number real images: 6993 / Average electron dose: 44.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 3.0 µm / Nominal defocus min: 1.0 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |