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- PDB-7mc0: Inward facing conformation of the MetNI methionine ABC transporter -

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Basic information

Entry
Database: PDB / ID: 7mc0
TitleInward facing conformation of the MetNI methionine ABC transporter
Components
  • ABC transporter, ATP-binding proteinATP-binding cassette transporter
  • ABC transporter, permease proteinATP-binding cassette transporter
KeywordsMEMBRANE PROTEIN
Function / homology
Function and homology information


D-methionine transmembrane transport / methionine transport / amino acid transport / ATPase-coupled transmembrane transporter activity / transmembrane transport / membrane => GO:0016020 / ATP binding / plasma membrane
Similarity search - Function
Methionine import ATP-binding protein MetN / Methionine import ATP-binding protein MetN, ATP-binding domain / ABC transporter type 1, transmembrane domain MetI-like / MetI-like superfamily / Binding-protein-dependent transport system inner membrane component / ABC transporter integral membrane type-1 domain profile. / ABC transporter-like, conserved site / ABC transporters family signature. / ABC transporter / ABC transporter-like, ATP-binding domain ...Methionine import ATP-binding protein MetN / Methionine import ATP-binding protein MetN, ATP-binding domain / ABC transporter type 1, transmembrane domain MetI-like / MetI-like superfamily / Binding-protein-dependent transport system inner membrane component / ABC transporter integral membrane type-1 domain profile. / ABC transporter-like, conserved site / ABC transporters family signature. / ABC transporter / ABC transporter-like, ATP-binding domain / ATP-binding cassette, ABC transporter-type domain profile. / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
ABC transporter, ATP-binding protein / ABC transporter, permease protein
Similarity search - Component
Biological speciesNeisseria meningitidis serogroup B (bacteria)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.3 Å
AuthorsSharaf, N.G. / Rees, D.C.
Funding support United States, 1items
OrganizationGrant numberCountry
Howard Hughes Medical Institute (HHMI) United States
CitationJournal: Elife / Year: 2021
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
DepositionApr 1, 2021Deposition site: RCSB / Processing site: RCSB
Revision 1.0Sep 1, 2021Provider: repository / Type: Initial release
Revision 1.1Sep 8, 2021Group: Data processing / Category: em_3d_reconstruction / Item: _em_3d_reconstruction.resolution

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Structure visualization

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Assembly

Deposited unit
A: ABC transporter, permease protein
B: ABC transporter, permease protein
C: ABC transporter, ATP-binding protein
D: ABC transporter, ATP-binding protein


Theoretical massNumber of molelcules
Total (without water)108,4584
Polymers108,4584
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_5551
Buried area6660 Å2
ΔGint-53 kcal/mol
Surface area43490 Å2

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Components

#1: Protein ABC transporter, permease protein / ATP-binding cassette transporter


Mass: 24363.064 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Neisseria meningitidis serogroup B (strain MC58) (bacteria)
Strain: MC58 / Gene: NMB1947 / Production host: Escherichia coli (E. coli) / References: UniProt: Q9JXP3
#2: Protein ABC transporter, ATP-binding protein / ATP-binding cassette transporter


Mass: 29866.152 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Neisseria meningitidis serogroup B (strain MC58) (bacteria)
Strain: MC58 / Gene: NMB1948 / Production host: Escherichia coli (E. coli) / References: UniProt: Q9JXP2

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: ABC transporter, permease protein, ABC transporter, ATP-binding proteinATP-binding cassette transporter
Type: COMPLEX / Entity ID: all / Source: RECOMBINANT
Molecular weight
IDEntity assembly-IDExperimental value
11NO
21NO
31NO
Source (natural)Organism: Neisseria meningitidis serogroup B (bacteria) / Strain: strain MC58
Source (recombinant)Organism: Escherichia coli (E. coli) / Strain: C43
Buffer solutionpH: 7.5
SpecimenConc.: 4.5 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Specimen supportGrid material: GOLD / Grid mesh size: 300 divisions/in. / Grid type: UltrAuFoil R1.2/1.3
VitrificationCryogen name: ETHANE

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: FEI TITAN KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELDBright-field microscopy
Image recordingElectron dose: 60 e/Å2 / Film or detector model: GATAN K3 (6k x 4k)
EM imaging opticsEnergyfilter name: GIF Bioquantum / Energyfilter slit width: 20 eV

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Processing

SoftwareName: PHENIX / Version: 1.18.2_3874: / Classification: refinement
EM software
IDNameCategory
12Cootmodel fitting
25ISOLDEmodel refinement
26Cootmodel refinement
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
3D reconstructionResolution: 3.3 Å / Num. of particles: 322171 / Symmetry type: POINT
Atomic model buildingProtocol: RIGID BODY FIT / Space: REAL / Target criteria: correlation coefficient
Atomic model buildingPDB-ID: 3TUJ

3tuj

Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.0067182
ELECTRON MICROSCOPYf_angle_d0.7089727
ELECTRON MICROSCOPYf_dihedral_angle_d11.2731007
ELECTRON MICROSCOPYf_chiral_restr0.0951190
ELECTRON MICROSCOPYf_plane_restr0.0031235

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