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- EMDB-66763: TamAB in non-hybrid barrel state -

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Open data


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Basic information

Entry
Database: EMDB / ID: EMD-66763
TitleTamAB in non-hybrid barrel state
Map data
Sample
  • Complex: complex of the translocation and assembly module A and B
    • Protein or peptide: Translocation and assembly module subunit TamA
    • Protein or peptide: Translocation and assembly module subunit TamB
Keywordsouter membrane / interaction / non-hybrid / TamAB / PROTEIN TRANSPORT / TamA / TamB / phospholipid transport / MEMBRANE PROTEIN
Function / homology
Function and homology information


TAM protein secretion complex / protein localization to outer membrane / protein secretion / cell outer membrane / plasma membrane
Similarity search - Function
Translocation and assembly module TamB / TamB C-terminal domain / TamA, POTRA domain 1 / POTRA domain TamA domain 1 / POTRA domain, BamA/TamA-like / Surface antigen variable number repeat / Surface antigen D15-like / POTRA domain / POTRA domain profile. / Bacterial surface antigen (D15) / Omp85 superfamily domain
Similarity search - Domain/homology
Translocation and assembly module subunit TamA / Translocation and assembly module subunit TamB
Similarity search - Component
Biological speciesEscherichia coli str. K-12 substr. MG1655 (bacteria)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.82 Å
AuthorsDong C / Zhang Z / Yang B
Funding support China, 1 items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC) China
CitationJournal: Nat Commun / Year: 2026
Title: Structural basis of outer membrane biogenesis by the TamAB translocase.
Authors: Biao Yang / Ruixin Fan / Mariana Bunoro Batista / Yatian Chen / Xiaofeng Duan / Rong Wang / Danyang Li / Phillip J Stansfeld / Zhengyu Zhang / Changjiang Dong /
Abstract: The outer membrane is vital for Gram-negative bacteria, playing crucial roles in colonization, pathogenesis and drug resistance. The translocation and assembly module A and B (TamAB) nanomachinery ...The outer membrane is vital for Gram-negative bacteria, playing crucial roles in colonization, pathogenesis and drug resistance. The translocation and assembly module A and B (TamAB) nanomachinery has been reported to be involved in transport of phospholipids from the inner membrane to the outer membrane, as well as insertion of critical outer membrane proteins. However, the underlying mechanisms remain poorly understood. Here we report cryogenic electron microscopy structures of TamAB in two conformations at resolutions of 3.69 and 3.82 Å. We reveal a hybrid barrel structure formed between the first β-strand of the TamA barrel and the last β-strand of the TamB C-terminal domain, which is folded inside the β-barrel. By integrating structural analysis with functional data, biochemical assays, and molecular dynamics simulations, we identify key residues involved in TamAB interactions and characterize the mechanisms of anterograde phospholipid transport within the continuously beta-helical hydrophobic cavity of TamB. Through disulfide bond crosslinking and functional assays, we reveal that TamA crosslinks with both TamB and Ag43. Additionally, we confirm that the two cryo-EM conformational states of TamAB exist in vivo. While BAM overexpression can compensate for TamAB deletion in Ag43 insertion, it does not rescue phospholipid transport. Given that TamA and TamB orthologs are widely distributed in among bacterial and eukaryotic organisms, our findings have broad implications in cell envelope biogenesis and offer potential avenues for therapeutic development through inhibition.
History
DepositionOct 27, 2025-
Header (metadata) releaseJan 28, 2026-
Map releaseJan 28, 2026-
UpdateFeb 18, 2026-
Current statusFeb 18, 2026Processing site: PDBc / Status: Released

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Structure visualization

Supplemental images

emd_66763.png

Downloads & links

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Map

FileDownload / File: emd_66763.map.gz / Format: CCP4 / Size: 244.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.84 Å/pix.
x 400 pix.
= 336. Å		0.84 Å/pix.
x 400 pix.
= 336. Å		0.84 Å/pix.
x 400 pix.
= 336. Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.84 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.1
Minimum - Maximum-0.73759997 - 1.0693218
Average (Standard dev.)-0.00015995567 (±0.013170814)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions400400400
Spacing400400400
CellA=B=C: 336.0 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_66763_msk_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #1

Fileemd_66763_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #2

Fileemd_66763_half_map_2.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
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Histogram

Histogram (log scale)

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Sample components

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Entire : complex of the translocation and assembly module A and B

EntireName: complex of the translocation and assembly module A and B
Components
  • Complex: complex of the translocation and assembly module A and B
    • Protein or peptide: Translocation and assembly module subunit TamA
    • Protein or peptide: Translocation and assembly module subunit TamB

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Supramolecule #1: complex of the translocation and assembly module A and B

SupramoleculeName: complex of the translocation and assembly module A and B
type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Escherichia coli str. K-12 substr. MG1655 (bacteria)

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Macromolecule #1: Translocation and assembly module subunit TamA

MacromoleculeName: Translocation and assembly module subunit TamA / type: protein_or_peptide / ID: 1
Details: The sequence of organism Escherichia coli str. K-12 substr. MG1655star is not available, replaced by P0ADE4 temporarily.
Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Escherichia coli str. K-12 substr. MG1655 (bacteria)
Molecular weightTheoretical: 64.842957 KDa
Recombinant expressionOrganism: Escherichia coli BL21(DE3) (bacteria)
SequenceString: VRYIRQLCCV SLLCLSGSAV AANVRLQVEG LSGQLEKNVR AQLSTIESDE VTPDRRFRAR VDDAIREGLK ALGYYQPTIE FDLRPPPKK GRQVLIAKVT PGVPVLIGGT DVVLRGGART DKDYLKLLDT RPAIGTVLNQ GDYENFKKSL TSIALRKGYF D SEFTKAQL ...String:
VRYIRQLCCV SLLCLSGSAV AANVRLQVEG LSGQLEKNVR AQLSTIESDE VTPDRRFRAR VDDAIREGLK ALGYYQPTIE FDLRPPPKK GRQVLIAKVT PGVPVLIGGT DVVLRGGART DKDYLKLLDT RPAIGTVLNQ GDYENFKKSL TSIALRKGYF D SEFTKAQL GIALGLHKAF WDIDYNSGER YRFGHVTFEG SQIRDEYLQN LVPFKEGDEY ESKDLAELNR RLSATGWFNS VV VAPQFDK ARETKVLPLT GVVSPRTENT IETGVGYSTD VGPRVKATWK KPWMNSYGHS LTTSTSISAP EQTLDFSYKM PLL KNPLEQ YYLVQGGFKR TDLNDTESDS TTLVASRYWD LSSGWQRAIN LRWSLDHFTQ GEITNTTMLF YPGVMISRTR SRGG LMPTW GDSQRYSIDY SNTAWGSDVD FSVFQAQNVW IRTLYDRHRF VTRGTLGWIE TGDFDKVPPD LRFFAGGDRS IRGYK YKSI APKYANGDLK GASKLITGSL EYQYNVTGKW WGAVFVDSGE AVSDIRRSDF KTGTGVGVRW ESPVGPIKLD FAVPVA DKD EHGLQFYIGL GPEL

UniProtKB: Translocation and assembly module subunit TamA

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Macromolecule #2: Translocation and assembly module subunit TamB

MacromoleculeName: Translocation and assembly module subunit TamB / type: protein_or_peptide / ID: 2
Details: MSLWKKISLGVVIVILLLLGSVAFLVGTTSGLHLVFKAADRWVPGLDIGKVTGGWRDLTLSDVRYEQPGVAVKAGNLHLA VGLECLWNSSVCINDLALKDIQVNIDSKKMPPSEQVEEEEDSGPLDLSTPYPITLTRVALDNVNIKIDDTTVSVMDFTSG ...Details: MSLWKKISLGVVIVILLLLGSVAFLVGTTSGLHLVFKAADRWVPGLDIGKVTGGWRDLTLSDVRYEQPGVAVKAGNLHLA VGLECLWNSSVCINDLALKDIQVNIDSKKMPPSEQVEEEEDSGPLDLSTPYPITLTRVALDNVNIKIDDTTVSVMDFTSG LNWQEKTLTLKPTSLKGLLIALPKVAEVAQEEVVEPKIENPQPDEKPLGETLKDLFSRPVLPEMTDVHLPLNLNIEEFKG EQLRVTGDTDITVSTMLLKVSSIDGNTKLDALDIDSSQGIVNASGTAQLSDNWPVDITLNSTLNVEPLKGEKVKLKMGGA LREQLEIGVNLSGPVDMDLRAQTRLAEAGLPLNVEVNSKQLYWPFTGEKQYQADDLKLKLTGKMTDYTLSMRTAVKGQEI PPATITLDAKGNEQQVNLDKLTVAALEGKTELKALLDWQQAISWRGELTLNGINTAKEFPDWPSKLNGLIKTRGSLYGGT WQMDVPELKLTGNVKQNKVNVDGTLKGNSYMQWMIPGLHLELGPNSAEVKGELGVKDLNLDATINAPGLDNALPGLGGTA KGLVKVRGTVEAPQLLADITARGLRWQELSVAQVRVEGDIKSTDQIAGKLDVRVEQISQPDVNINLVTLNAKGSEKQHEL QLRIQGEPVSGQLNLAGSFDRKEERWKGTLSNTRFQTPVGPWSLTRDIALDYRNKEQKISIGPHCWLNPNAELCVPQTID AGAEGRAVVNLNRFDLAMLKPFMPETTQASGIFTGKADVAWDTTKEGLPQGSITLSGRNVQVTQTVNDAALPVAFQTLNL TAELRNNRAELGWTIRLTNNGQFDGQVQVTDPQGRRNLGGNVNIRNFNLAMINPIFTRGEKAAGMVSANLRLGGDVQSPQ LFGQLQVTGVDIDGNFMPFDMQPSQLAVNFNGMRSTLAGTVRTQQGEIYLNGDADWSQIENWRARVTAKGSKVRITVPPM VRMDVSPDVVFEATPNLFTLDGRVDVPWARIVVHDLPESAVGVSSDVVMLNDNLQPEEPKTASIPINSNLIVHVGNNVRI DAFGLKARLTGDLNVVQDKQGLGLNGQINIPEGRFHAYGQDLIVRKGELLFSGPPDQPYLNIEAIRNPDATEDDVIAGVR VTGLADEPKAEIFSDPAMSQQAALSYLLRGQGLESDQSDSAAMTSMLIGLGVAQSGQIVGKIGETFGVSNLALDTQGVGD SSQVVVSGYVLPGLQVKYGVGIFDSIATLTLRYRLMPKLYLEAVSGVDQALDLLYQFEF
Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Escherichia coli str. K-12 substr. MG1655 (bacteria)
Molecular weightTheoretical: 136.905062 KDa
Recombinant expressionOrganism: Escherichia coli BL21(DE3) (bacteria)
SequenceString: MSLWKKISLG VVIVILLLLG SVAFLVGTTS GLHLVFKAAD RWVPGLDIGK VTGGWRDLTL SDVRYEQPGV AVKAGNLHLA VGLECLWNS SVCINDLALK DIQVNIDSKK MPPSEQVEEE EDSGPLDLST PYPITLTRVA LDNVNIKIDD TTVSVMDFTS G LNWQEKTL ...String:
MSLWKKISLG VVIVILLLLG SVAFLVGTTS GLHLVFKAAD RWVPGLDIGK VTGGWRDLTL SDVRYEQPGV AVKAGNLHLA VGLECLWNS SVCINDLALK DIQVNIDSKK MPPSEQVEEE EDSGPLDLST PYPITLTRVA LDNVNIKIDD TTVSVMDFTS G LNWQEKTL TLKPTSLKGL LIALPKVAEV AQEEVVEPKI ENPQPDEKPL GETLKDLFSR PVLPEMTDVH LPLNLNIEEF KG EQLRVTG DTDITVSTML LKVSSIDGNT KLDALDIDSS QGIVNASGTA QLSDNWPVDI TLNSTLNVEP LKGEKVKLKM GGA LREQLE IGVNLSGPVD MDLRAQTRLA EAGLPLNVEV NSKQLYWPFT GEKQYQADDL KLKLTGKMTD YTLSMRTAVK GQEI PPATI TLDAKGNEQQ VNLDKLTVAA LEGKTELKAL LDWQQAISWR GELTLNGINT AKEFPDWPSK LNGLIKTRGS LYGGT WQMD VPELKLTGNV KQNKVNVDGT LKGNSYMQWM IPGLHLELGP NSAEVKGELG VKDLNLDATI NAPGLDNALP GLGGTA KGL VKVRGTVEAP QLLADITARG LRWQELSVAQ VRVEGDIKST DQIAGKLDVR VEQISQPDVN INLVTLNAKG SEKQHEL QL RIQGEPVSGQ LNLAGSFDRK EERWKGTLSN TRFQTPVGPW SLTRDIALDY RNKEQKISIG PHCWLNPNAE LCVPQTID A GAEGRAVVNL NRFDLAMLKP FMPETTQASG IFTGKADVAW DTTKEGLPQG SITLSGRNVQ VTQTVNDAAL PVAFQTLNL TAELRNNRAE LGWTIRLTNN GQFDGQVQVT DPQGRRNLGG NVNIRNFNLA MINPIFTRGE KAAGMVSANL RLGGDVQSPQ LFGQLQVTG VDIDGNFMPF DMQPSQLAVN FNGMRSTLAG TVRTQQGEIY LNGDADWSQI ENWRARVTAK GSKVRITVPP M VRMDVSPD VVFEATPNLF TLDGRVDVPW ARIVVHDLPE SAVGVSSDVV MLNDNLQPEE PKTASIPINS NLIVHVGNNV RI DAFGLKA RLTGDLNVVQ DKQGLGLNGQ INIPEGRFHA YGQDLIVRKG ELLFSGPPDQ PYLNIEAIRN PDATEDDVIA GVR VTGLAD EPKAEIFSDP AMSQQAALSY LLRGQGLESD QSDSAAMTSM LIGLGVAQSG QIVGKIGETF GVSNLALDTQ GVGD SSQVV VSGYVLPGLQ VKYGVGIFDS IATLTLRYRL MPKLYLEAVS GVDQALDLLY QFEF

UniProtKB: Translocation and assembly module subunit TamB

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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: 8
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 50.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: OTHER / Imaging mode: BRIGHT FIELD / Nominal defocus max: 3.0 µm / Nominal defocus min: 1.0 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: INSILICO MODEL
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.82 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC (ver. 4.5.3) / Number images used: 110592
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
FSC plot (resolution estimation)

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