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- EMDB-23751: Outward facing conformation of the MetNI methionine ABC transport... -
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Open data
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Basic information
Entry | Database: EMDB / ID: EMD-23751 | |||||||||
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Title | Outward facing conformation of the MetNI methionine ABC transporter in complex with lipo-MetQ | |||||||||
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Function / homology | ![]() D-methionine transmembrane transport / transmembrane transport / ![]() ![]() ![]() ![]() Similarity search - Function | |||||||||
Biological species | ![]() ![]() ![]() ![]() | |||||||||
Method | ![]() ![]() | |||||||||
![]() | Sharaf NG / Rees DC | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Characterization of the ABC methionine transporter from reveals that lipidated MetQ is required for interaction. Authors: Naima G Sharaf / Mona Shahgholi / Esther Kim / Jeffrey Y Lai / David G VanderVelde / Allen T Lee / Douglas C Rees / ![]() Abstract: NmMetQ is a substrate-binding protein (SBP) from that has been identified as a surface-exposed candidate antigen for meningococcal vaccines. However, this location for NmMetQ challenges the ...NmMetQ is a substrate-binding protein (SBP) from that has been identified as a surface-exposed candidate antigen for meningococcal vaccines. However, this location for NmMetQ challenges the prevailing view that SBPs in Gram-negative bacteria are localized to the periplasmic space to promote interaction with their cognate ABC transporter embedded in the bacterial inner membrane. To elucidate the roles of NmMetQ, we characterized NmMetQ with and without its cognate ABC transporter (NmMetNI). Here, we show that NmMetQ is a lipoprotein (lipo-NmMetQ) that binds multiple methionine analogs and stimulates the ATPase activity of NmMetNI. Using single-particle electron cryo-microscopy, we determined the structures of NmMetNI in the presence and absence of lipo-NmMetQ. Based on our data, we propose that NmMetQ tethers to membranes via a lipid anchor and has dual function and localization, playing a role in NmMetNI-mediated transport at the inner membrane and moonlighting on the bacterial surface. | |||||||||
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 | ![]() | 229.7 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 12.4 KB 12.4 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 14.5 KB | Display | ![]() |
Images | ![]() | 29.6 KB | ||
Filedesc metadata | ![]() | 5.7 KB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 7mbzMC ![]() 7mc0C 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 | sharpened map | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 0.856 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 : ABC transporter, permease protein, Lipoprotein, ABC transporter, ...
Entire | Name: ABC transporter, permease protein, Lipoprotein, ABC transporter, ATP-binding protein![]() |
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Components |
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-Supramolecule #1: ABC transporter, permease protein, Lipoprotein, ABC transporter, ...
Supramolecule | Name: ABC transporter, permease protein, Lipoprotein, ABC transporter, ATP-binding protein type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() ![]() |
-Macromolecule #1: ABC transporter, permease protein
Macromolecule | Name: ABC transporter, permease protein / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() Strain: MC58 |
Molecular weight | Theoretical: 24.363064 KDa |
Recombinant expression | Organism: ![]() ![]() ![]() |
Sequence | String: MADLTFQQAV STIVGMKDEI FRALGETFVM VGLSTTFAVI FGTLLGVLLF VTSSRQLHYN KLVNFLLDNL VNLMRAFPFV ILMIAMIPA TRAIVGSTIG PVAASLVLSV SGLFYFARLV EQNLREVPKG VIEAAAAMGA PPIAIVCKVL LNEARAGMVS S ITVLAIGL ...String: MADLTFQQAV STIVGMKDEI FRALGETFVM VGLSTTFAVI FGTLLGVLLF VTSSRQLHYN KLVNFLLDNL VNLMRAFPFV ILMIAMIPA TRAIVGSTIG PVAASLVLSV SGLFYFARLV EQNLREVPKG VIEAAAAMGA PPIAIVCKVL LNEARAGMVS S ITVLAIGL LSYSAAAGMI GGGGLGDLAI RYGYYRYQTE VIIFIVALLV LLVILIQSTG NALARKLDKR UniProtKB: ![]() |
-Macromolecule #2: Lipoprotein
Macromolecule | Name: Lipoprotein / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() Strain: MC58 |
Molecular weight | Theoretical: 33.010246 KDa |
Recombinant expression | Organism: ![]() ![]() ![]() |
Sequence | String: MKTFFKTLSA AALALILAAC GGQKDSAPAA SASAAADNGA AKKEIVFGTT VGDFGDMVKE QIQAELEKKG YTVKLVEFTD YVRPNLALA EGELDINVFQ HKPYLDDFKK EHNLDITEVF QVPTAPLGLY PGKLKSLEEV KDGSTVSAPN DPSNFARVLV M LDELGWIK ...String: MKTFFKTLSA AALALILAAC GGQKDSAPAA SASAAADNGA AKKEIVFGTT VGDFGDMVKE QIQAELEKKG YTVKLVEFTD YVRPNLALA EGELDINVFQ HKPYLDDFKK EHNLDITEVF QVPTAPLGLY PGKLKSLEEV KDGSTVSAPN DPSNFARVLV M LDELGWIK LKDGINPLTA SKADIAENLK NIKIVELEAA QLPRSRADVD FAVVNGNYAI SSGMKLTEAL FQEPSFAYVN WS AVKTADK DSQWLKDVTE AYNSDAFKAY AHKRFEGYKS PAAWNEGAAK KLEHHHHHHH HHH UniProtKB: ![]() |
-Macromolecule #3: ABC transporter, ATP-binding protein
Macromolecule | Name: ABC transporter, ATP-binding protein / type: protein_or_peptide / ID: 3 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() Strain: MC58 |
Molecular weight | Theoretical: 29.866152 KDa |
Recombinant expression | Organism: ![]() ![]() ![]() |
Sequence | String: MGHHHHHHHH HHSSGHIDDD DKHMIILDKV SKHYQTRDKT RFAAVEPTSL EIRDGEIFGL MGYSGAGKST LLRLINLLER PDSGKVNVC GQELTALDAA ALRQARQNIG MVFQQFNLLS NRTVADNVAF PLEIAGWPSE KIKARVKECL EIVGLTERAG H YPAQLSGG ...String: MGHHHHHHHH HHSSGHIDDD DKHMIILDKV SKHYQTRDKT RFAAVEPTSL EIRDGEIFGL MGYSGAGKST LLRLINLLER PDSGKVNVC GQELTALDAA ALRQARQNIG MVFQQFNLLS NRTVADNVAF PLEIAGWPSE KIKARVKECL EIVGLTERAG H YPAQLSGG QKQRVGIARA LAPKPQVILA DEPTSALDPA TTRSVLECLE DINKRFNVTI VIVTHEMSVI RRLCDRAALL DK GKVVEIV EVRGNQIHAQ SDIGRELIRE D UniProtKB: ![]() |
-Experimental details
-Structure determination
Method | ![]() |
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Aggregation state | particle |
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Sample preparation
Concentration | 4.5 mg/mL |
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Buffer | pH: 7.5 |
Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD![]() |
Specialist optics | Energy filter - Name: GIF Bioquantum / Energy filter - Slit width: 20 eV |
Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 60.0 e/Å2 |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
-Atomic model buiding 1
Refinement | Space: REAL / Protocol: RIGID BODY FIT / Target criteria: correlation coefficient |
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Output model | ![]() PDB-7mbz: |