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- EMDB-30526: the Acinetobacter MlaFEDB complex in ATP-bound Vtrans1 conformation -
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Open data
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Basic information
Entry | Database: EMDB / ID: EMD-30526 | |||||||||
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Title | the Acinetobacter MlaFEDB complex in ATP-bound Vtrans1 conformation | |||||||||
![]() | cryo EM map of the MlaFEDB complex in ATP-bound Vtrans1 conformation | |||||||||
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![]() | MEMBRANE PROTEIN | |||||||||
Function / homology | ![]() phospholipid transporter activity / ATP-binding cassette (ABC) transporter complex / phospholipid binding / ATP hydrolysis activity / extracellular region / ATP binding / membrane Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 4.0 Å | |||||||||
![]() | Zhang YY / Fan QX | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Cryo-EM structures of Acinetobacter baumannii glycerophospholipid transporter. Authors: Yuanyuan Zhang / Qiongxuan Fan / Ximin Chi / Qiang Zhou / Yanyan Li / ![]() | |||||||||
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 | ![]() | 28.5 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 13.4 KB 13.4 KB | Display Display | ![]() |
Images | ![]() | 50.7 KB | ||
Filedesc metadata | ![]() | 5.5 KB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 551.1 KB | Display | ![]() |
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Full document | ![]() | 550.7 KB | Display | |
Data in XML | ![]() | 5.6 KB | Display | |
Data in CIF | ![]() | 6.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 7d08MC ![]() 7d06C ![]() 7d09C ![]() 7d0aC M: atomic model generated by this map C: citing same article ( |
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Similar structure data |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
File | ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Annotation | cryo EM map of the MlaFEDB complex in ATP-bound Vtrans1 conformation | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.087 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
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Sample components
-Entire : Acinetobacter MlaFEDB complex in ATP-bound Vtrans1 conformation
Entire | Name: Acinetobacter MlaFEDB complex in ATP-bound Vtrans1 conformation |
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Components |
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-Supramolecule #1: Acinetobacter MlaFEDB complex in ATP-bound Vtrans1 conformation
Supramolecule | Name: Acinetobacter MlaFEDB complex in ATP-bound Vtrans1 conformation type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#4 |
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Source (natural) | Organism: ![]() |
-Macromolecule #1: Intermembrane phospholipid transport system permease protein MlaE
Macromolecule | Name: Intermembrane phospholipid transport system permease protein MlaE type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 27.322443 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MNTIAWLGRL VIERIRGIGV AALMLLQIIF SLPSAGGFGR FVYQMHRVGV MSLLIITVSG LFIGLVLGLQ GYSILVNVGS ESMLGTMVS LTLLRELAPV VAALLFAGRA GSALTAEIGS MKQSEQLASM EMIGVDPLKQ IVSPRLWAGI VSLPMLTVIF A AIGIVGGK ...String: MNTIAWLGRL VIERIRGIGV AALMLLQIIF SLPSAGGFGR FVYQMHRVGV MSLLIITVSG LFIGLVLGLQ GYSILVNVGS ESMLGTMVS LTLLRELAPV VAALLFAGRA GSALTAEIGS MKQSEQLASM EMIGVDPLKQ IVSPRLWAGI VSLPMLTVIF A AIGIVGGK LVGVDFLGVD EGSFWSGMQN NVQFGHDVVN GIIKSIVFAL LCTWIAVFQG YACDPTPEGI ATAMTRTVVY SS LCVLGFD FVLTAVMFGG I UniProtKB: Intermembrane phospholipid transport system permease protein MlaE |
-Macromolecule #2: ABC transporter ATP-binding protein
Macromolecule | Name: ABC transporter ATP-binding protein / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 30.070455 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MMNNKTPLST QSLIEVKNLS FNRGERVIYD NISLNIRRGQ ITAIMGPSGT GKTTLLRLIG GQLVPDQGEV LLDGKDIAQM SRQELFAAR ARMGMLFQSG ALFTDMSVYE NVAFPIRAHT KLSENLIAEL VALKLESVGL RGTEQLMPTE LSGGMNRRVA L ARAIALDP ...String: MMNNKTPLST QSLIEVKNLS FNRGERVIYD NISLNIRRGQ ITAIMGPSGT GKTTLLRLIG GQLVPDQGEV LLDGKDIAQM SRQELFAAR ARMGMLFQSG ALFTDMSVYE NVAFPIRAHT KLSENLIAEL VALKLESVGL RGTEQLMPTE LSGGMNRRVA L ARAIALDP DLIMYDEPFA GQDPIVKGVL TRLIRSLREA LDLTTIIVSH DVPETLSIAD YIYVVAEGKI QGEGTPEELQ AY ASPFVKQ FLTGSAEGPV EYQFSHQAYL DNEVRP UniProtKB: ABC transporter ATP-binding protein |
-Macromolecule #3: Anti-sigma factor antagonist
Macromolecule | Name: Anti-sigma factor antagonist / type: protein_or_peptide / ID: 3 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 11.91376 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: VVQYLNQELV VSGKIDFENA EQQYQAGLAI IKKQTSFPLI VDLKQLEHGN TLALAVLVQW LRQTPQKSGL HFKNVPEKML KIIQACHLQ EDLHLVLEHH HHHH UniProtKB: Anti-sigma factor antagonist |
-Macromolecule #4: MCE family protein
Macromolecule | Name: MCE family protein / type: protein_or_peptide / ID: 4 / Number of copies: 6 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 23.672824 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MKSRTSELAV GIFVIIFGIA LFFLAMKVSG LVGTNLSDGY TMKAQFDNVN GLKPRAKVTM SGVTIGRVDS ITLDPVTRLA TVTFDLDGK LTSFNAEQLK EVQKNALDEL RYSSDYTQAT PAQQKTMEQQ LISNMNSITS IDEDAYIMVA TNGLLGEKYL K IVPGGGLN ...String: MKSRTSELAV GIFVIIFGIA LFFLAMKVSG LVGTNLSDGY TMKAQFDNVN GLKPRAKVTM SGVTIGRVDS ITLDPVTRLA TVTFDLDGK LTSFNAEQLK EVQKNALDEL RYSSDYTQAT PAQQKTMEQQ LISNMNSITS IDEDAYIMVA TNGLLGEKYL K IVPGGGLN YLKRGDTISN TQGTMDLEDL ISKFITGGGA GKVAAGSSSA EEKAPASTDS SAQP UniProtKB: ABC transporter periplasmic substrate-binding protein |
-Macromolecule #5: ADENOSINE-5'-TRIPHOSPHATE
Macromolecule | Name: ADENOSINE-5'-TRIPHOSPHATE / type: ligand / ID: 5 / Number of copies: 2 / Formula: ATP |
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Molecular weight | Theoretical: 507.181 Da |
Chemical component information | ![]() ChemComp-ATP: |
-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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Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 50.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
Startup model | Type of model: OTHER |
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Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 4.0 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 3.0.6) / Number images used: 48606 |
Initial angle assignment | Type: OTHER |
Final angle assignment | Type: MAXIMUM LIKELIHOOD |