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- EMDB-14715: S-layer Deinoxanthin Binding Complex, C3 symmetry -

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Entry
Database: EMDB / ID: EMD-14715
TitleS-layer Deinoxanthin Binding Complex, C3 symmetry
Map dataComplex C3 symmetry
Sample
  • Complex: S-layer Deinoxanthin Binding Complex, C3 Symmetry
    • Protein or peptide: S-layer protein SlpA
  • Ligand: (3~{S},5~{R},6~{R})-5-[(3~{S},7~{R},12~{S},16~{S},20~{S})-3,7,12,16,20,24-hexamethyl-24-oxidanyl-pentacosyl]-4,4,6-trimethyl-cyclohexane-1,3-diol
  • Ligand: [(2~{S})-2-acetyloxy-3-[[(2~{S})-3-[(2~{R},3~{S},4~{S},5~{S},6~{S})-6-(hydroxymethyl)-3-(octadecanoylamino)-4,5-bis(oxidanyl)oxan-2-yl]oxy-1-oxidanylidene-1-(pentylamino)propan-2-yl]oxy-oxidanyl-phosphoryl]oxy-propyl] ethanoate
  • Ligand: [(2~{S})-3-[[(2~{S})-3-[(2~{S},3~{S},4~{S},5~{S},6~{S})-6-(hydroxymethyl)-4,5-bis(oxidanyl)-3-(propanoylamino)oxan-2-yl]oxy-1-oxidanylidene-1-(pentadecylamino)propan-2-yl]oxy-oxidanyl-phosphoryl]oxy-2-octanoyloxy-propyl] decanoate
  • Ligand: COPPER (II) ION
  • Ligand: FE (III) ION
KeywordsPROTEIN / STRUCTURAL PROTEIN / S-layer / deinococcus radiodurans / DR_2577 / S-layer Deinoxanthin Binding Complex
Function / homology
Function and homology information


porin activity / pore complex / monoatomic ion transport / cell outer membrane / lipid binding
Similarity search - Function
: / S-layer protein SlpA, beta-barrel / : / S-layer homology domain / S-layer homology domain / S-layer homology (SLH) domain profile. / Prokaryotic membrane lipoprotein lipid attachment site profile.
Similarity search - Domain/homology
Outer membrane protein SlpA / CHRD domain-containing protein
Similarity search - Component
Biological speciesDeinococcus radiodurans R1 (radioresistant)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.54 Å
AuthorsFarci D / Piano D
Funding support Poland, 2 items
OrganizationGrant numberCountry
Polish National Science CentrePRO-2017/26/E/NZ1/00344 Poland
Polish National Science CentrePRO-2018/30/M/NZ1/00284 Poland
CitationJournal: J Biol Chem / Year: 2022
Title: The cryo-EM structure of the S-layer deinoxanthin-binding complex of Deinococcus radiodurans informs properties of its environmental interactions.
Authors: Domenica Farci / Patrycja Haniewicz / Daniele de Sanctis / Luca Iesu / Sami Kereïche / Mathias Winterhalter / Dario Piano /
Abstract: The radiation-resistant bacterium Deinococcus radiodurans is known as the world's toughest bacterium. The S-layer of D. radiodurans, consisting of several proteins on the surface of the cellular ...The radiation-resistant bacterium Deinococcus radiodurans is known as the world's toughest bacterium. The S-layer of D. radiodurans, consisting of several proteins on the surface of the cellular envelope and intimately associated with the outer membrane, has therefore been useful as a model for structural and functional studies. Its main proteinaceous unit, the S-layer deinoxanthin-binding complex (SDBC), is a hetero-oligomeric assembly known to contribute to the resistance against environmental stress and have porin functional features; however, its precise structure is unknown. Here, we resolved the structure of the SDBC at ∼2.5 Å resolution by cryo-EM and assigned the sequence of its main subunit, the protein DR_2577. This structure is characterized by a pore region, a massive β-barrel organization, a stalk region consisting of a trimeric coiled coil, and a collar region at the base of the stalk. We show that each monomer binds three Cu ions and one Fe ion and retains one deinoxanthin molecule and two phosphoglycolipids, all exclusive to D. radiodurans. Finally, electrophysiological characterization of the SDBC shows that it exhibits transport properties with several amino acids. Taken together, these results highlight the SDBC as a robust structure displaying both protection and sieving functions that facilitates exchanges with the environment.
History
DepositionApr 4, 2022-
Header (metadata) releaseJul 13, 2022-
Map releaseJul 13, 2022-
UpdateJul 24, 2024-
Current statusJul 24, 2024Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_14715.png

Downloads & links

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Map

FileDownload / File: emd_14715.map.gz / Format: CCP4 / Size: 561.5 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationComplex C3 symmetry
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.82 Å/pix.
x 528 pix.
= 431.904 Å		0.82 Å/pix.
x 528 pix.
= 431.904 Å		0.82 Å/pix.
x 528 pix.
= 431.904 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.818 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.46
Minimum - Maximum-1.6617153 - 2.9926715
Average (Standard dev.)0.001637759 (±0.05989737)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions528528528
Spacing528528528
CellA=B=C: 431.90402 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: Complex C3 Half map A

Fileemd_14715_half_map_1.map
AnnotationComplex C3 Half map A
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Complex C3 Half map B

Fileemd_14715_half_map_2.map
AnnotationComplex C3 Half map B
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : S-layer Deinoxanthin Binding Complex, C3 Symmetry

EntireName: S-layer Deinoxanthin Binding Complex, C3 Symmetry
Components
  • Complex: S-layer Deinoxanthin Binding Complex, C3 Symmetry
    • Protein or peptide: S-layer protein SlpA
  • Ligand: (3~{S},5~{R},6~{R})-5-[(3~{S},7~{R},12~{S},16~{S},20~{S})-3,7,12,16,20,24-hexamethyl-24-oxidanyl-pentacosyl]-4,4,6-trimethyl-cyclohexane-1,3-diol
  • Ligand: [(2~{S})-2-acetyloxy-3-[[(2~{S})-3-[(2~{R},3~{S},4~{S},5~{S},6~{S})-6-(hydroxymethyl)-3-(octadecanoylamino)-4,5-bis(oxidanyl)oxan-2-yl]oxy-1-oxidanylidene-1-(pentylamino)propan-2-yl]oxy-oxidanyl-phosphoryl]oxy-propyl] ethanoate
  • Ligand: [(2~{S})-3-[[(2~{S})-3-[(2~{S},3~{S},4~{S},5~{S},6~{S})-6-(hydroxymethyl)-4,5-bis(oxidanyl)-3-(propanoylamino)oxan-2-yl]oxy-1-oxidanylidene-1-(pentadecylamino)propan-2-yl]oxy-oxidanyl-phosphoryl]oxy-2-octanoyloxy-propyl] decanoate
  • Ligand: COPPER (II) ION
  • Ligand: FE (III) ION

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Supramolecule #1: S-layer Deinoxanthin Binding Complex, C3 Symmetry

SupramoleculeName: S-layer Deinoxanthin Binding Complex, C3 Symmetry / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1
Source (natural)Organism: Deinococcus radiodurans R1 (radioresistant)
Molecular weightTheoretical: 800 KDa

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Macromolecule #1: S-layer protein SlpA

MacromoleculeName: S-layer protein SlpA / type: protein_or_peptide / ID: 1 / Number of copies: 3 / Enantiomer: LEVO
Source (natural)Organism: Deinococcus radiodurans R1 (radioresistant)
Strain: ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422
Molecular weightTheoretical: 123.835367 KDa
SequenceString: MKKSLIALTT ALSFGLAAAQ TAAPVSAPQV PALTDVPAGH WAKDAIDRLV SRGVILGYPD GTFRGTQNLT RYEAAIIIAR LLDQMRDGE TPAGMTAEDM TALQNAIQEL AADLAALGVR VSDLEANAVS KDDFARLEAR IEEVAAAGGE QGATEALQGQ I DDLTARVD ...String:
MKKSLIALTT ALSFGLAAAQ TAAPVSAPQV PALTDVPAGH WAKDAIDRLV SRGVILGYPD GTFRGTQNLT RYEAAIIIAR LLDQMRDGE TPAGMTAEDM TALQNAIQEL AADLAALGVR VSDLEANAVS KDDFARLEAR IEEVAAAGGE QGATEALQGQ I DDLTARVD EYDALRADVD DNASSIAALN DLTVLLNQDI LDLQDRVSAV EAAQADFVQR SDFDALGGRV TTVETRVETV NN SLTGRIA ALERNAFSVK PSLTIGYSVS RTSRNFDVDR LFPLNADGTV ANNAFTSGGI DTDTGAQRRD FGDFGNASDP VVA GAAGLY GFADGVSYTV YFTDGSTATF DGLNPADYKV PTGKVIDTTK GRNGFGFNNL ARYKEGSTDI GISLGFDTSG QFSQ VTSGT GGSLFSTAGR LQVNQIDLNF GLVTGLPSDA YVDTNGNGKK DDGEATGRGT YLGSGGTAAI LRDPAGNVYR PVFFR FKNA TTQFSVGNNP VIVTLGQQQK FYFSDYVFDN NYDGRGDGFT VTVDGSNVPV IGAWKPQIKG VYGSRSGLDG TAEAGY GVY YRGVRAQITP VGTLTAGIHY AQEGRDMFGA AQNTTSTPSD VTTYGADLHG KAFGVELHSE YATSRVRPNT ANAAVQT SN AFYARVATRK DNLAFDLNTP AAKFGNDTFG VSLYDLNYRK IDAGYNNVAG ISEYGYGSYS RTSAQNIAYN PDTGVTAP F ANLDRQAYTD ANNDGTSDRN ADGTVVATNT KIGQMGFGVK AAANLGPVAI GGYYDTSTGA NGDNANRMTE AGGSAKVAY SIFSLRGTYN TLDSNRPQIY RDAAGTQIIG DAKVRRYAVQ ADVTPGLGLF VGAYYRDVNV NGVRSTTDRG LLGRGYLASS FEPGVGNNA YRTGLRCADN NFGTGTRDID GVGGVLNPAV NLDQSRTATC FTSYGVEAGH AGDNANALVK DLFFRVGYSR V YVPTTATA TTGDFSGSVT YGDARYDRKV GVANVRLAGS FSTTNTQLDS RPAGTRGAVG LIVRTDPLEN VPFRPQFNGQ VG YYTADNR VAAGNYNANA TKYGAGVVLN DFLLPQTKIG VRYDGYMAQN RQYTPFDGDG TQGYFSDANN NRRTNLNGVY VEG AYQDLI FSYGTYTLSQ KDLNGVEYGS GINNGQPARG QTFKISYKVN F

UniProtKB: Outer membrane protein SlpA

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Macromolecule #2: (3~{S},5~{R},6~{R})-5-[(3~{S},7~{R},12~{S},16~{S},20~{S})-3,7,12,...

MacromoleculeName: (3~{S},5~{R},6~{R})-5-[(3~{S},7~{R},12~{S},16~{S},20~{S})-3,7,12,16,20,24-hexamethyl-24-oxidanyl-pentacosyl]-4,4,6-trimethyl-cyclohexane-1,3-diol
type: ligand / ID: 2 / Number of copies: 3 / Formula: JPI
Molecular weightTheoretical: 609.061 Da
Chemical component information

ChemComp-JPI:
(3~{S},5~{R},6~{R})-5-[(3~{S},7~{R},12~{S},16~{S},20~{S})-3,7,12,16,20,24-hexamethyl-24-oxidanyl-pentacosyl]-4,4,6-trimethyl-cyclohexane-1,3-diol

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Macromolecule #3: [(2~{S})-2-acetyloxy-3-[[(2~{S})-3-[(2~{R},3~{S},4~{S},5~{S},6~{S...

MacromoleculeName: [(2~{S})-2-acetyloxy-3-[[(2~{S})-3-[(2~{R},3~{S},4~{S},5~{S},6~{S})-6-(hydroxymethyl)-3-(octadecanoylamino)-4,5-bis(oxidanyl)oxan-2-yl]oxy-1-oxidanylidene-1-(pentylamino)propan-2-yl]oxy- ...Name: [(2~{S})-2-acetyloxy-3-[[(2~{S})-3-[(2~{R},3~{S},4~{S},5~{S},6~{S})-6-(hydroxymethyl)-3-(octadecanoylamino)-4,5-bis(oxidanyl)oxan-2-yl]oxy-1-oxidanylidene-1-(pentylamino)propan-2-yl]oxy-oxidanyl-phosphoryl]oxy-propyl] ethanoate
type: ligand / ID: 3 / Number of copies: 3 / Formula: JQ6
Molecular weightTheoretical: 840.975 Da
Chemical component information

ChemComp-JQ6:
[(2~{S})-2-acetyloxy-3-[[(2~{S})-3-[(2~{R},3~{S},4~{S},5~{S},6~{S})-6-(hydroxymethyl)-3-(octadecanoylamino)-4,5-bis(oxidanyl)oxan-2-yl]oxy-1-oxidanylidene-1-(pentylamino)propan-2-yl]oxy-oxidanyl-phosphoryl]oxy-propyl] ethanoate

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Macromolecule #4: [(2~{S})-3-[[(2~{S})-3-[(2~{S},3~{S},4~{S},5~{S},6~{S})-6-(hydrox...

MacromoleculeName: [(2~{S})-3-[[(2~{S})-3-[(2~{S},3~{S},4~{S},5~{S},6~{S})-6-(hydroxymethyl)-4,5-bis(oxidanyl)-3-(propanoylamino)oxan-2-yl]oxy-1-oxidanylidene-1-(pentadecylamino)propan-2-yl]oxy-oxidanyl- ...Name: [(2~{S})-3-[[(2~{S})-3-[(2~{S},3~{S},4~{S},5~{S},6~{S})-6-(hydroxymethyl)-4,5-bis(oxidanyl)-3-(propanoylamino)oxan-2-yl]oxy-1-oxidanylidene-1-(pentadecylamino)propan-2-yl]oxy-oxidanyl-phosphoryl]oxy-2-octanoyloxy-propyl] decanoate
type: ligand / ID: 4 / Number of copies: 3 / Formula: JPX
Molecular weightTheoretical: 967.214 Da
Chemical component information

ChemComp-JPX:
[(2~{S})-3-[[(2~{S})-3-[(2~{S},3~{S},4~{S},5~{S},6~{S})-6-(hydroxymethyl)-4,5-bis(oxidanyl)-3-(propanoylamino)oxan-2-yl]oxy-1-oxidanylidene-1-(pentadecylamino)propan-2-yl]oxy-oxidanyl-phosphoryl]oxy-2-octanoyloxy-propyl] decanoate

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Macromolecule #5: COPPER (II) ION

MacromoleculeName: COPPER (II) ION / type: ligand / ID: 5 / Number of copies: 9 / Formula: CU
Molecular weightTheoretical: 63.546 Da
Chemical component information

ChemComp-CU:
COPPER (II) ION

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Macromolecule #6: FE (III) ION

MacromoleculeName: FE (III) ION / type: ligand / ID: 6 / Number of copies: 3 / Formula: FE
Molecular weightTheoretical: 55.845 Da

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 7.4
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K2 QUANTUM (4k x 4k) / Average electron dose: 1.3 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: SPOT SCAN / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.0 µm / Nominal defocus min: 0.5 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: NONE
Final reconstructionApplied symmetry - Point group: C3 (3 fold cyclic) / Resolution.type: BY AUTHOR / Resolution: 2.54 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 252122
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
FSC plot (resolution estimation)

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