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- PDB-7ssu: Structure of EmrE-D3 mutant in complex with monobody L10 and meth... -

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Basic information

Entry
Database: PDB / ID: 7ssu
TitleStructure of EmrE-D3 mutant in complex with monobody L10 and methyltriphenylphosphonium
Components
  • L10 monobody
  • Multidrug transporter EmrE
KeywordsTRANSPORT PROTEIN/IMMUNE SYSTEM / Small Multidrug Resistance transporters / drug efflux pump / EmrE / Membrane protein / TRANSPORT PROTEIN-IMMUNE SYSTEM complex
Function / homology
Function and homology information


EmrE multidrug transporter complex / glycine betaine transport / amino-acid betaine transmembrane transporter activity / choline transmembrane transporter activity / choline transport / xenobiotic detoxification by transmembrane export across the plasma membrane / antiporter activity / response to osmotic stress / xenobiotic transport / xenobiotic transmembrane transporter activity ...EmrE multidrug transporter complex / glycine betaine transport / amino-acid betaine transmembrane transporter activity / choline transmembrane transporter activity / choline transport / xenobiotic detoxification by transmembrane export across the plasma membrane / antiporter activity / response to osmotic stress / xenobiotic transport / xenobiotic transmembrane transporter activity / transmembrane transporter activity / xenobiotic metabolic process / transmembrane transport / cellular response to xenobiotic stimulus / response to xenobiotic stimulus / DNA damage response / identical protein binding / membrane / plasma membrane
Similarity search - Function
Small drug/metabolite transporter protein family / Small multidrug resistance protein / Small Multidrug Resistance protein
Similarity search - Domain/homology
methyltriphenylphosphonium / Multidrug transporter EmrE
Similarity search - Component
Biological speciesEscherichia coli (E. coli)
Homo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.22 Å
AuthorsKermani, A.A. / Stockbridge, R.B.
Funding support United States, 1items
OrganizationGrant numberCountry
National Science Foundation (NSF, United States)1845012 United States
CitationJournal: Elife / Year: 2022
Title: Crystal structures of bacterial small multidrug resistance transporter EmrE in complex with structurally diverse substrates.
Authors: Kermani, A.A. / Burata, O.E. / Koff, B.B. / Koide, A. / Koide, S. / Stockbridge, R.B.
History
DepositionNov 11, 2021Deposition site: RCSB / Processing site: RCSB
Revision 1.0Mar 2, 2022Provider: repository / Type: Initial release
Revision 1.1May 18, 2022Group: Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _citation_author.identifier_ORCID
Revision 1.2Oct 18, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Multidrug transporter EmrE
C: L10 monobody
B: Multidrug transporter EmrE
D: L10 monobody
hetero molecules


Theoretical massNumber of molelcules
Total (without water)43,9565
Polymers43,6784
Non-polymers2771
Water00
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4760 Å2
ΔGint-43 kcal/mol
Surface area20150 Å2
Unit cell
Length a, b, c (Å)141.171, 50.870, 110.799
Angle α, β, γ (deg.)90.000, 92.690, 90.000
Int Tables number5
Space group name H-MC121

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Components

#1: Protein Multidrug transporter EmrE / Efflux-multidrug resistance protein EmrE / Ethidium resistance protein / Methyl viologen resistance protein C


Mass: 11907.279 Da / Num. of mol.: 2 / Mutation: E25N, W31I, V34M
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (strain K12) (bacteria)
Strain: K12 / Gene: emrE, eb, mvrC, b0543, JW0531 / Plasmid: pET-21c / Production host: Escherichia coli BL21(DE3) (bacteria) / Variant (production host): C41 / References: UniProt: P23895
#2: Antibody L10 monobody


Mass: 9931.934 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli BL21(DE3) (bacteria)
#3: Chemical ChemComp-B5J / methyltriphenylphosphonium


Mass: 277.320 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C19H18P / Feature type: SUBJECT OF INVESTIGATION
Has ligand of interestY

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 4.69 Å3/Da / Density % sol: 73.79 %
Crystal growTemperature: 294 K / Method: vapor diffusion, sitting drop / pH: 6.5
Details: 0.1 M lithium nitrate, 0.1 M ADA, pH 6.5, 33% PEG600

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Data collection

DiffractionMean temperature: 80 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 21-ID-D / Wavelength: 0.9183 Å
DetectorType: DECTRIS EIGER X 9M / Detector: PIXEL / Date: Sep 27, 2021
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9183 Å / Relative weight: 1
ReflectionResolution: 3.22→70.5 Å / Num. obs: 8969 / % possible obs: 88.6 % / Redundancy: 6.6 % / CC1/2: 0.967 / Rmerge(I) obs: 0.152 / Rsym value: 0.166 / Net I/σ(I): 10.4
Reflection shellResolution: 3.22→3.42 Å / Rmerge(I) obs: 0.656 / Num. unique obs: 448 / CC1/2: 0.861 / Rrim(I) all: 0.707 / % possible all: 13.22

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Processing

Software
NameVersionClassification
Aimlessdata scaling
PHASERphasing
PHENIX1.18.2-3874-000refinement
PDB_EXTRACTdata extraction
Cootmodel building
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB entry 6WK8

6wk8


Resolution: 3.22→58.24 Å / SU ML: 0.48 / Cross valid method: THROUGHOUT / σ(F): 1.38 / Phase error: 38.71 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.3328 389 4.85 %
Rwork0.2925 --
obs0.2944 8025 61.76 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 157.42 Å2 / Biso mean: 78.5449 Å2 / Biso min: 29.3 Å2
Refinement stepCycle: final / Resolution: 3.22→58.24 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2940 0 20 0 2960
Biso mean--84.59 --
Num. residues----384
LS refinement shellResolution: 3.22→3.34 Å /
RfactorNum. reflection
Rfree0.4114 -
Rwork0.3877 -
all-167

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