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- EMDB-40682: The cryo-EM structure of the EcBAM/EspP(beta1-12) complex -

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Basic information

Entry
Database: EMDB / ID: EMD-40682
TitleThe cryo-EM structure of the EcBAM/EspP(beta1-12) complex
Map dataThe cryo-EM structure of the EcBAM/EspP(beta1-12) complex
Sample
  • Complex: BAM/EspP(beta1-12)
    • Protein or peptide: Outer membrane protein assembly factor BamA
    • Protein or peptide: Outer membrane protein assembly factor BamB
    • Protein or peptide: Outer membrane protein assembly factor BamC
    • Protein or peptide: Outer membrane protein assembly factor BamD
    • Protein or peptide: Outer membrane protein assembly factor BamE
    • Protein or peptide: Serine protease EspP
Keywordsmembrane proteins / protein folding / BAM complex / outer membrane protein / MEMBRANE PROTEIN / MEMBRANE PROTEIN-Hydrolase complex
Function / homology
Function and homology information


Bam protein complex / Gram-negative-bacterium-type cell outer membrane assembly / protein insertion into membrane / Hydrolases; Acting on peptide bonds (peptidases); Serine endopeptidases / cell outer membrane / periplasmic space / serine-type endopeptidase activity / cell surface / proteolysis / extracellular region ...Bam protein complex / Gram-negative-bacterium-type cell outer membrane assembly / protein insertion into membrane / Hydrolases; Acting on peptide bonds (peptidases); Serine endopeptidases / cell outer membrane / periplasmic space / serine-type endopeptidase activity / cell surface / proteolysis / extracellular region / membrane / identical protein binding
Similarity search - Function
Peptidase S6, IgA endopeptidase / Peptidase family S6 domain / Immunoglobulin A1 protease / Peptidase family S6 domain profile. / Autotransporter beta-domain / Outer membrane autotransporter barrel / Autotransporter beta-domain / Autotransporter beta-domain profile. / Autotransporter beta-domain / Autotransporter beta-domain superfamily ...Peptidase S6, IgA endopeptidase / Peptidase family S6 domain / Immunoglobulin A1 protease / Peptidase family S6 domain profile. / Autotransporter beta-domain / Outer membrane autotransporter barrel / Autotransporter beta-domain / Autotransporter beta-domain profile. / Autotransporter beta-domain / Autotransporter beta-domain superfamily / Outer membrane protein assembly factor BamB / NlpB/DapX lipoprotein / Outer membrane protein assembly factor BamC / Outer membrane protein assembly factor BamC, C-terminal / NlpB/DapX lipoprotein / Autotransporter, pectate lyase C-like domain superfamily / Outer membrane protein assembly factor BamD / Outer membrane protein assembly factor BamE / Lipoprotein SmpA/OmlA / Outer membrane lipoprotein BamD-like / SmpA / OmlA family / Outer membrane lipoprotein / BamE-like / Outer membrane protein assembly factor BamA / Pyrrolo-quinoline quinone repeat / PQQ-like domain / POTRA domain, BamA/TamA-like / Surface antigen variable number repeat / POTRA domain / POTRA domain profile. / Pyrrolo-quinoline quinone beta-propeller repeat / beta-propeller repeat / Surface antigen D15-like / Bacterial surface antigen (D15) / Omp85 superfamily domain / Quinoprotein alcohol dehydrogenase-like superfamily / Pectin lyase fold/virulence factor / Prokaryotic membrane lipoprotein lipid attachment site profile. / Tetratricopeptide-like helical domain superfamily / WD40/YVTN repeat-like-containing domain superfamily
Similarity search - Domain/homology
Outer membrane protein assembly factor BamE / Outer membrane protein assembly factor BamD / Outer membrane protein assembly factor BamA / Outer membrane protein assembly factor BamC / Outer membrane protein assembly factor BamB / Serine protease EspP
Similarity search - Component
Biological speciesEscherichia coli (E. coli) / Escherichia coli 0.1288 (bacteria) / Escherichia coli O157 (bacteria)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.9 Å
AuthorsWu R / Noinaj N
Funding support United States, 3 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)1R01GM127884 United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)1R01GM127896 United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)1R01GM123169 United States
CitationJournal: To Be Published
Title: BAM orchestrates OMP biogenesis using a beta-templating mechanism
Authors: Wu R / Ryoo D / Kuo KM / Gumbart JC / Noinaj N
History
DepositionMay 3, 2023-
Header (metadata) releaseMay 8, 2024-
Map releaseMay 8, 2024-
UpdateMay 8, 2024-
Current statusMay 8, 2024Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_40682.png

Downloads & links

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Map

FileDownload / File: emd_40682.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationThe cryo-EM structure of the EcBAM/EspP(beta1-12) complex
Voxel sizeX=Y=Z: 1.08 Å
Density
Contour LevelBy AUTHOR: 0.35
Minimum - Maximum-1.7115021 - 2.5004163
Average (Standard dev.)0.0035667638 (±0.064137585)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions256256256
Spacing256256256
CellA=B=C: 276.48 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: Half Map 1

Fileemd_40682_half_map_1.map
AnnotationHalf Map 1
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Half Map 2

Fileemd_40682_half_map_2.map
AnnotationHalf Map 2
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : BAM/EspP(beta1-12)

EntireName: BAM/EspP(beta1-12)
Components
  • Complex: BAM/EspP(beta1-12)
    • Protein or peptide: Outer membrane protein assembly factor BamA
    • Protein or peptide: Outer membrane protein assembly factor BamB
    • Protein or peptide: Outer membrane protein assembly factor BamC
    • Protein or peptide: Outer membrane protein assembly factor BamD
    • Protein or peptide: Outer membrane protein assembly factor BamE
    • Protein or peptide: Serine protease EspP

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Supramolecule #1: BAM/EspP(beta1-12)

SupramoleculeName: BAM/EspP(beta1-12) / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Escherichia coli (E. coli)

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Macromolecule #1: Outer membrane protein assembly factor BamA

MacromoleculeName: Outer membrane protein assembly factor BamA / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Escherichia coli (E. coli)
Molecular weightTheoretical: 88.247477 KDa
Recombinant expressionOrganism: Escherichia coli BL21(DE3) (bacteria)
SequenceString: FVVKDIHFEG LQRVAVGAAL LSMPVRTGDT VNDEDISNTI RALFATGNFE DVRVLRDGDT LLVQVKERPT IASITFSGNK SVKDDMLKQ NLEASGVRVG ESLDRTTIAD IEKGLEDFYY SVGKYSASVK AVVTPLPRNR VDLKLVFQEG VSAEIQQINI V GNHAFTTD ...String:
FVVKDIHFEG LQRVAVGAAL LSMPVRTGDT VNDEDISNTI RALFATGNFE DVRVLRDGDT LLVQVKERPT IASITFSGNK SVKDDMLKQ NLEASGVRVG ESLDRTTIAD IEKGLEDFYY SVGKYSASVK AVVTPLPRNR VDLKLVFQEG VSAEIQQINI V GNHAFTTD ELISHFQLRD EVPWWNVVGD RKYQKQKLAG DLETLRSYYL DRGYARFNID STQVSLTPDK KGIYVTVNIT EG DQYKLSG VEVSGNLAGH SAEIEQLTKI EPGELYNGTK VTKMEDDIKK LLGRYGYAYP RVQSMPEIND ADKTVKLRVN VDA GNRFYV RKIRFEGNDT SKDAVLRREM RQMEGAWLGS DLVDQGKERL NRLGFFETVD TDTQRVPGSP DQVDVVYKVK ERNT GSFNF GIGYGTESGV SFQAGVQQDN WLGTGYAVGI NGTKNDYQTY AELSVTNPYF TVDGVSLGGR LFYNDFQADD ADLSD YTNK SYGTDVTLGF PINEYNSLRA GLGYVHNSLS NMQPQVAMWR YLYSMGEHPS TSDQDNSFKT DDFTFNYGWT YNKLDR GYF PTDGSRVNLT GKVTIPGSDN EYYKVTLDTA TYVPIDDDHK WVVLGRTRWG YGDGLGGKEM PFYENFYAGG SSTVRGF QS NTIGPKAVYF PHQASNYDPD YDYECATQDG AKDLCKSDDA VGGNAMAVAS LEFITPTPFI SDKYANSVRT SFFWDMGT V WDTNWDSSQY SGYPDYSDPS NIRMSAGIAL QWMSPLGPLV FSYAQPFKKY DGDKAEQFQF NCGKTW

UniProtKB: Outer membrane protein assembly factor BamA

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Macromolecule #2: Outer membrane protein assembly factor BamB

MacromoleculeName: Outer membrane protein assembly factor BamB / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Escherichia coli (E. coli)
Molecular weightTheoretical: 39.77923 KDa
Recombinant expressionOrganism: Escherichia coli BL21(DE3) (bacteria)
SequenceString: SLFNSEEDVV KMSPLPTVEN QFTPTTAWST SVGSGIGNFY SNLHPALADN VVYAADRAGL VKALNADDGK EIWSVSLAEK DGWFSKEPA LLSGGVTVSG GHVYIGSEKA QVYALNTSDG TVAWQTKVAG EALSRPVVSD GLVLIHTSNG QLQALNEADG A VKWTVNLD ...String:
SLFNSEEDVV KMSPLPTVEN QFTPTTAWST SVGSGIGNFY SNLHPALADN VVYAADRAGL VKALNADDGK EIWSVSLAEK DGWFSKEPA LLSGGVTVSG GHVYIGSEKA QVYALNTSDG TVAWQTKVAG EALSRPVVSD GLVLIHTSNG QLQALNEADG A VKWTVNLD MPSLSLRGES APTTAFGAAV VGGDNGRVSA VLMEQGQMIW QQRISQATGS TEIDRLSDVD TTPVVVNGVV FA LAYNGNL TALDLRSGQI MWKRELGSVN DFIVDGNRIY LVDQNDRVMA LTIDGGVTLW TQSDLLHRLL TSPVLYNGNL VVG DSEGYL HWINVEDGRF VAQQKVDSSG FQTEPVAADG KLLIQAKDGT VYSITR

UniProtKB: Outer membrane protein assembly factor BamB

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Macromolecule #3: Outer membrane protein assembly factor BamC

MacromoleculeName: Outer membrane protein assembly factor BamC / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Escherichia coli 0.1288 (bacteria)
Molecular weightTheoretical: 34.298109 KDa
Recombinant expressionOrganism: Escherichia coli BL21(DE3) (bacteria)
SequenceString: SSDSRYKRQV SGDEAYLEAA PLAELHAPAG MILPVTSGDY AIPVTNGSGA VGKALDIRPP AQPLALVSGA RTQFTGDTAS LLVENGRGN TLWPQVVSVL QAKNYTITQR DDAGQTLTTD WVQWNRLDED EQYRGRYQIS VKPQGYQQAV TVKLLNLEQA G KPVADAAS ...String:
SSDSRYKRQV SGDEAYLEAA PLAELHAPAG MILPVTSGDY AIPVTNGSGA VGKALDIRPP AQPLALVSGA RTQFTGDTAS LLVENGRGN TLWPQVVSVL QAKNYTITQR DDAGQTLTTD WVQWNRLDED EQYRGRYQIS VKPQGYQQAV TVKLLNLEQA G KPVADAAS MQRYSTEMMN VISAGLDKSA TDAANAAQNR ASTTMDVQSA ADDTGLPMLV VRGPFNVVWQ RLPAALEKVG MK VTDSTRS QGNMAVTYKP LSDSDWQELG ASDPGLASGD YKLQVGDLDN RSSLQFIDPK GHTLTQSQND ALVAVFQAAF SK

UniProtKB: Outer membrane protein assembly factor BamC

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Macromolecule #4: Outer membrane protein assembly factor BamD

MacromoleculeName: Outer membrane protein assembly factor BamD / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Escherichia coli (E. coli)
Molecular weightTheoretical: 25.713676 KDa
Recombinant expressionOrganism: Escherichia coli BL21(DE3) (bacteria)
SequenceString: SGSKEEVPDN PPNEIYATAQ QKLQDGNWRQ AITQLEALDN RYPFGPYSQQ VQLDLIYAYY KNADLPLAQA AIDRFIRLNP THPNIDYVM YMRGLTNMAL DDSALQGFFG VDRSDRDPQH ARAAFSDFSK LVRGYPNSQY TTDATKRLVF LKDRLAKYEY S VAEYYTER ...String:
SGSKEEVPDN PPNEIYATAQ QKLQDGNWRQ AITQLEALDN RYPFGPYSQQ VQLDLIYAYY KNADLPLAQA AIDRFIRLNP THPNIDYVM YMRGLTNMAL DDSALQGFFG VDRSDRDPQH ARAAFSDFSK LVRGYPNSQY TTDATKRLVF LKDRLAKYEY S VAEYYTER GAWVAVVNRV EGMLRDYPDT QATRDALPLM ENAYRQMQMN AQAEKVAKII AANSSNT

UniProtKB: Outer membrane protein assembly factor BamD

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Macromolecule #5: Outer membrane protein assembly factor BamE

MacromoleculeName: Outer membrane protein assembly factor BamE / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Escherichia coli (E. coli)
Molecular weightTheoretical: 10.540661 KDa
Recombinant expressionOrganism: Escherichia coli BL21(DE3) (bacteria)
SequenceString:
STLERVVYRP DINQGNYLTA NDVSKIRVGM TQQQVAYALG TPLMSDPFGT NTWFYVFRQQ PGHEGVTQQT LTLTFNSSGV LTNIDNKPA LSGNGGH

UniProtKB: Outer membrane protein assembly factor BamE

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Macromolecule #6: Serine protease EspP

MacromoleculeName: Serine protease EspP / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO
EC number: Hydrolases; Acting on peptide bonds (peptidases); Serine endopeptidases
Source (natural)Organism: Escherichia coli O157 (bacteria)
Molecular weightTheoretical: 38.77384 KDa
Recombinant expressionOrganism: Escherichia coli BL21(DE3) (bacteria)
SequenceString: GSIELVSAPK DTNENVFKAS KQTIGFSDVT PVITTRETDD KITWSLTGYN TVANKEATRN AAALFSVDYK AFLNEVSNLN KRMGDLRDI NGEAGCWARI MSGTGSASGG FSDNYTHVQV GVDKKHELDG LDLFTGFTVT HTDSSASADV FSGKTKSVGA G LYASAMFD ...String:
GSIELVSAPK DTNENVFKAS KQTIGFSDVT PVITTRETDD KITWSLTGYN TVANKEATRN AAALFSVDYK AFLNEVSNLN KRMGDLRDI NGEAGCWARI MSGTGSASGG FSDNYTHVQV GVDKKHELDG LDLFTGFTVT HTDSSASADV FSGKTKSVGA G LYASAMFD SGAYIDLIGK YVHHDNEYTA TFAGLGTRDY STHSWYAGAE AGYRYHVTED AWIEPQAELV YGSVSGKQFA WK DQGMHLS MKDKDYNPLI GRTGVDVGKS FSGKDWKVTA RAGLGYQFDL LANGETVLRD ASGEKRIKGE KDSRMLMSVG LNA EIRDNV RFGLEFEKSA FGKYNVDNAV NANFRYSF

UniProtKB: Serine protease EspP

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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 %

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Cs: 2.7 mm / Nominal defocus max: 2.5 µm / Nominal defocus min: 1.5 µm
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 53.47 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: NONE
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.9 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 145290

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