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Open data
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Basic information
Entry | Database: EMDB / ID: EMD-10831 | |||||||||
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Title | Structure of S. oneidensis MotAB | |||||||||
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Function / homology | ![]() | |||||||||
Biological species | ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.48 Å | |||||||||
![]() | Santiveri M / Roa-Eguiara A / Taylor NMI | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Structure and Function of Stator Units of the Bacterial Flagellar Motor. Authors: Mònica Santiveri / Aritz Roa-Eguiara / Caroline Kühne / Navish Wadhwa / Haidai Hu / Howard C Berg / Marc Erhardt / Nicholas M I Taylor / ![]() ![]() ![]() Abstract: Many bacteria use the flagellum for locomotion and chemotaxis. Its bidirectional rotation is driven by a membrane-embedded motor, which uses energy from the transmembrane ion gradient to generate ...Many bacteria use the flagellum for locomotion and chemotaxis. Its bidirectional rotation is driven by a membrane-embedded motor, which uses energy from the transmembrane ion gradient to generate torque at the interface between stator units and rotor. The structural organization of the stator unit (MotAB), its conformational changes upon ion transport, and how these changes power rotation of the flagellum remain unknown. Here, we present ~3 Å-resolution cryoelectron microscopy reconstructions of the stator unit in different functional states. We show that the stator unit consists of a dimer of MotB surrounded by a pentamer of MotA. Combining structural data with mutagenesis and functional studies, we identify key residues involved in torque generation and present a detailed mechanistic model for motor function and switching of rotational direction. | |||||||||
History |
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Structure visualization
Movie |
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Structure viewer | EM map: ![]() ![]() ![]() |
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 59.8 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 14.8 KB 14.8 KB | Display Display | ![]() |
Images | ![]() | 86.6 KB | ||
Masks | ![]() | 64 MB | ![]() | |
Others | ![]() ![]() | 59.4 MB 59.4 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
EMDB pages | ![]() ![]() |
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Map
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Voxel size | X=Y=Z: 0.832 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Mask #1
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_10831_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #2
File | emd_10831_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
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Sample components
-Entire : Stator unit MotAB
Entire | Name: Stator unit MotAB |
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Components |
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-Supramolecule #1: Stator unit MotAB
Supramolecule | Name: Stator unit MotAB / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all Details: The stator unit consists of a dimer of MotB surrounded by a pentamer of MotA. |
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Source (natural) | Organism: ![]() |
Recombinant expression | Organism: ![]() ![]() |
-Macromolecule #1: MotA
Macromolecule | Name: MotA / type: protein_or_peptide / ID: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MSFIGVIVAL VFILVGNLIE GGHPSALLDL PAFMIVIGGT IGATVAQFPF SVIIASMKRF KWLIFPLRTD LNERAEFLIE IAGDVRKGGL LSIEDKIDQI DDPFLHKGLE LLVDGYEKDN IVEILEKEIE FEQHGIEQTV KVYEAMGGYC PTMGIVGAVF GLIHAMGLLD ...String: MSFIGVIVAL VFILVGNLIE GGHPSALLDL PAFMIVIGGT IGATVAQFPF SVIIASMKRF KWLIFPLRTD LNERAEFLIE IAGDVRKGGL LSIEDKIDQI DDPFLHKGLE LLVDGYEKDN IVEILEKEIE FEQHGIEQTV KVYEAMGGYC PTMGIVGAVF GLIHAMGLLD APDKLGGAIA VAFIATIYGV AAANIIFLPF GNRYKAFAHQ LSLFKEMTLT GITGIADGES PQRLQAQLNP YLEH |
-Macromolecule #2: MotB
Macromolecule | Name: MotB / type: protein_or_peptide / ID: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MKKKKVDPPE NHERWLISYA DFMTLLFALF VVLYSFAMSD KNEAKFMVEG LIDSLSKIGL ISTPAVNALA PGGTSILEPN TVTSAVDAEP KLIETATTAP STSESNNDLT NAKSNDTIRK YKEIISAKLK NEIENQEVEI DEVSDNLIIR IGDNNTFFAS GSAFIQPKFI ...String: MKKKKVDPPE NHERWLISYA DFMTLLFALF VVLYSFAMSD KNEAKFMVEG LIDSLSKIGL ISTPAVNALA PGGTSILEPN TVTSAVDAEP KLIETATTAP STSESNNDLT NAKSNDTIRK YKEIISAKLK NEIENQEVEI DEVSDNLIIR IGDNNTFFAS GSAFIQPKFI PLIDKIGEVI ASVPGRVVIA GHTDATLPME IYADNWDLSS LRATAVVRIM TKNKGVNPSR IIVQGLADTQ PRFQNDTPEH RQKNRRIEII LNQGNTVESH IPIPEGTLEV LFQGPGGSGS AWSHPQFEKG GGSGGGSGGS AWSHPQFEK |
-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: 8 |
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Grid | Model: Quantifoil R2/1 / Pretreatment - Type: GLOW DISCHARGE |
Vitrification | Cryogen name: ETHANE / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: FEI FALCON III (4k x 4k) / Detector mode: COUNTING / Average electron dose: 40.84 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
Final reconstruction | Applied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 3.48 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC / Number images used: 799093 |
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Initial angle assignment | Type: OTHER |
Final angle assignment | Type: PROJECTION MATCHING |