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Yorodumi- PDB-6z5u: Cryo-EM structure of the A. baumannii MlaBDEF complex bound to APPNHP -
+Open data
-Basic information
Entry | Database: PDB / ID: 6z5u | ||||||
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Title | Cryo-EM structure of the A. baumannii MlaBDEF complex bound to APPNHP | ||||||
Components |
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Keywords | MEMBRANE PROTEIN / lipid transport / antibiotic resistance / ABC transporter | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Acinetobacter baumannii (bacteria) | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.9 Å | ||||||
Authors | Mann, D. / Bergeron, J.R.C. | ||||||
Funding support | United Kingdom, 1items
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Citation | Journal: Commun Biol / Year: 2021 Title: Structure and lipid dynamics in the maintenance of lipid asymmetry inner membrane complex of A. baumannii. Authors: Daniel Mann / Junping Fan / Kamolrat Somboon / Daniel P Farrell / Andrew Muenks / Svetomir B Tzokov / Frank DiMaio / Syma Khalid / Samuel I Miller / Julien R C Bergeron / Abstract: Multi-resistant bacteria are a major threat in modern medicine. The gram-negative coccobacillus Acinetobacter baumannii currently leads the WHO list of pathogens in critical need for new therapeutic ...Multi-resistant bacteria are a major threat in modern medicine. The gram-negative coccobacillus Acinetobacter baumannii currently leads the WHO list of pathogens in critical need for new therapeutic development. The maintenance of lipid asymmetry (MLA) protein complex is one of the core machineries that transport lipids from/to the outer membrane in gram-negative bacteria. It also contributes to broad-range antibiotic resistance in several pathogens, most prominently in A. baumannii. Nonetheless, the molecular details of its role in lipid transport has remained largely elusive. Here, we report the cryo-EM maps of the core MLA complex, MlaBDEF, from the pathogen A. baumannii, in the apo-, ATP- and ADP-bound states, revealing multiple lipid binding sites in the cytosolic and periplasmic side of the complex. Molecular dynamics simulations suggest their potential trajectory across the membrane. Collectively with the recently-reported structures of the E. coli orthologue, this data also allows us to propose a molecular mechanism of lipid transport by the MLA system. #1: Journal: Biorxiv / Year: 2020 Title: Structure and lipid dynamics in the A. baumannii maintenance of lipid asymmetry (MLA) inner membrane complex Authors: Mann, D. / Fan, J. / Farrell, D.P. / Somboon, K. / Muenks, A. / Tzokov, S.B. / Khalid, S. / Dimaio, F. / Miller, S.I. / Bergeron, J.R.C. | ||||||
History |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | Molecule: MolmilJmol/JSmol |
-Downloads & links
-Download
PDBx/mmCIF format | 6z5u.cif.gz | 384 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6z5u.ent.gz | 314.7 KB | Display | PDB format |
PDBx/mmJSON format | 6z5u.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/z5/6z5u ftp://data.pdbj.org/pub/pdb/validation_reports/z5/6z5u | HTTPS FTP |
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-Related structure data
Related structure data | 11082MC M: map data used to model this data C: citing same article (ref.) |
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Similar structure data | |
EM raw data | EMPIAR-10425 (Title: Cryo-EM structure of the A.baumannii MlaBDEF complex bound to AppNHp Data size: 135.6 Data #1: MotionCor2 aligned micrographs [micrographs - single frame]) |
-Links
-Assembly
Deposited unit |
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1 |
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-Components
-ABC transporter ... , 2 types, 4 molecules ABKL
#1: Protein | Mass: 27322.443 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Acinetobacter baumannii (bacteria) Gene: mlaE, ttg2B, A7M79_03105, A7M90_14775, ABCAM1_3325, APD33_11020, B4R90_07005, B9X95_19830, BGC29_10505, C2U32_12245, CHQ89_09020, CPI82_03200, DLI75_08555, E5294_02070, E5979_07650, EA685_ ...Gene: mlaE, ttg2B, A7M79_03105, A7M90_14775, ABCAM1_3325, APD33_11020, B4R90_07005, B9X95_19830, BGC29_10505, C2U32_12245, CHQ89_09020, CPI82_03200, DLI75_08555, E5294_02070, E5979_07650, EA685_00455, EA706_02625, EA722_02115, EA746_009620, EKS29_03575, EWO92_15675, EWO96_10890, EWP49_16265, FD887_10930, FJU42_03310, FJU87_05505, FJV14_14505, FR761_17360, LV38_01098, SAMEA104305261_03368, SAMEA104305351_00191 Production host: Escherichia coli (E. coli) / References: UniProt: V5V9F4 #4: Protein | Mass: 30367.848 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Acinetobacter baumannii (bacteria) / Gene: ttg2A, NU60_03710 / Production host: Escherichia coli (E. coli) / References: UniProt: A0A4P2WWN2 |
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-Protein , 2 types, 8 molecules CDEGHIJF
#2: Protein | Mass: 10874.672 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Acinetobacter baumannii (bacteria) Gene: mlaB, A7M79_03090, A7M90_14790, A9843_11720, AA954_03140, ABCAM1_3322, ABUW_0387, APD33_11035, B4R90_07020, B9W69_03450, B9X95_19845, BGC29_10490, C2U32_12230, CEJ64_02055, CHQ89_09005, CPI82_ ...Gene: mlaB, A7M79_03090, A7M90_14790, A9843_11720, AA954_03140, ABCAM1_3322, ABUW_0387, APD33_11035, B4R90_07020, B9W69_03450, B9X95_19845, BGC29_10490, C2U32_12230, CEJ64_02055, CHQ89_09005, CPI82_03185, CSB70_3293, DLI69_20965, DLI75_08570, DOL94_03255, DVA79_09290, E2533_15225, E2536_07480, E5294_02085, E5979_07665, EA685_00440, EA686_18495, EA706_02640, EA722_02130, EA746_009635, EKS29_03590, EWO92_15660, EWO96_10875, EWP49_16250, FD887_10915, FD913_07380, FJU36_09990, FJU42_03325, FJU76_08875, FJU79_12020, FJU87_05520, FJV14_14520, FR761_17345, LV38_01095, NCTC13305_02846, NCTC13420_03382, SAMEA104305261_03371, SAMEA104305351_00188 Production host: Escherichia coli (E. coli) / References: UniProt: V5V9K5 #3: Protein | Mass: 24135.322 Da / Num. of mol.: 6 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Acinetobacter baumannii (bacteria) Gene: mlaD, ttg2C, A7M79_03100, A7M90_14780, A9843_11730, AA954_03130, ABCAM1_3324, ABUW_0385, APD33_11025, B4R90_07010, B9W69_03440, B9X95_19835, BGC29_10500, C2U32_12240, CEJ64_02065, CHQ89_09015, ...Gene: mlaD, ttg2C, A7M79_03100, A7M90_14780, A9843_11730, AA954_03130, ABCAM1_3324, ABUW_0385, APD33_11025, B4R90_07010, B9W69_03440, B9X95_19835, BGC29_10500, C2U32_12240, CEJ64_02065, CHQ89_09015, CPI82_03195, CSB70_3295, DLI69_20975, DLI75_08560, DOL94_03245, DVA79_09280, E2533_15215, E2536_07470, E5294_02075, E5979_07655, EA685_00450, EA706_02630, EA722_02120, EA746_009625, EKS29_03580, EWO92_15670, EWO96_10885, EWP49_16260, FD887_10925, FD913_07390, FJU36_10000, FJU76_08865, FJU79_12010, FJU87_05510, FJV14_14510, FR761_17355, LV38_01097, NCTC13305_02844, NCTC13420_03380, SAMEA104305318_02183, SAMEA104305351_00190 Production host: Escherichia coli (E. coli) / References: UniProt: V5V921 |
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-Non-polymers , 2 types, 4 molecules
#5: Chemical | #6: Chemical | |
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-Details
Has ligand of interest | N |
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-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
-Sample preparation
Component | Name: MlaBDEF complex / Type: COMPLEX / Entity ID: #1-#4 / Source: RECOMBINANT |
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Molecular weight | Experimental value: NO |
Source (natural) | Organism: Acinetobacter baumannii (bacteria) |
Source (recombinant) | Organism: Escherichia coli (E. coli) |
Buffer solution | pH: 7 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Vitrification | Cryogen name: ETHANE |
-Electron microscopy imaging
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: FEI TITAN KRIOS |
Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: SPOT SCAN |
Electron lens | Mode: BRIGHT FIELDBright-field microscopy |
Image recording | Electron dose: 47 e/Å2 / Film or detector model: GATAN K2 SUMMIT (4k x 4k) |
-Processing
CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
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3D reconstruction | Resolution: 3.9 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 93295 / Symmetry type: POINT |