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Open data
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Basic information
| Entry | ![]() | |||||||||
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| Title | BAM-SurA complex (P2-visible 1) | |||||||||
Map data | ||||||||||
Sample |
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Keywords | Outer membrane protein / Periplasmic chaperon / PROTEIN TRANSPORT | |||||||||
| Function / homology | Function and homology informationBam protein complex / Gram-negative-bacterium-type cell outer membrane assembly / Secretion of toxins / protein insertion into membrane / peptide binding / peptidylprolyl isomerase / peptidyl-prolyl cis-trans isomerase activity / cell outer membrane / outer membrane-bounded periplasmic space / protein folding ...Bam protein complex / Gram-negative-bacterium-type cell outer membrane assembly / Secretion of toxins / protein insertion into membrane / peptide binding / peptidylprolyl isomerase / peptidyl-prolyl cis-trans isomerase activity / cell outer membrane / outer membrane-bounded periplasmic space / protein folding / protein-macromolecule adaptor activity / protein stabilization / cell surface / membrane / identical protein binding Similarity search - Function | |||||||||
| Biological species | ![]() | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.04 Å | |||||||||
Authors | Kohga H / Miyazaki R / Nugraha Y / Tsukazaki T | |||||||||
| Funding support | Japan, 1 items
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Citation | Journal: Nat Commun / Year: 2026Title: Cryo-EM structures of the SurA-BAM complex reveal conformational changes in outer membrane protein assembly. Authors: Ryoji Miyazaki / Hidetaka Kohga / Nami Matsuoka / Yuki Maruno / Wataru Yoshimoto / Yutaro S Takahashi / Dede Heri Yuli Yanto / Yudhi Nugraha / Hideki Shigematsu / Takuya Shiota / Tomoya Tsukazaki / ![]() Abstract: The outer membrane (OM) of Gram-negative bacteria acts as a permeability barrier against toxic compounds. Its integrity is maintained by various outer membrane proteins (OMPs), which are inserted ...The outer membrane (OM) of Gram-negative bacteria acts as a permeability barrier against toxic compounds. Its integrity is maintained by various outer membrane proteins (OMPs), which are inserted into the OM by the β-barrel assembly machinery (BAM) complex. The periplasmic chaperone SurA delivers unfolded OMPs to BAM; however, the mechanism of substrate transfer remains unclear. Here, we show that the flexible P1 and P2 domains of SurA regulate the function of its Core domain and interact with BAM components, including BamE, whose interaction with the P2 domain is crucial for efficient OMP assembly. Moreover, cryo-electron microscopy reveals four distinct Escherichia coli SurA-BAM structures, suggesting dynamic domain rearrangements of SurA. Based on these findings, we propose a dynamic model in which SurA transfers substrates to BAM through multiple conformational changes, providing a unified framework for chaperone-assisted OMP biogenesis. | |||||||||
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Structure visualization
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_66834.map.gz | 153.3 MB | EMDB map data format | |
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| Header (meta data) | emd-66834-v30.xml emd-66834.xml | 23.2 KB 23.2 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_66834_fsc.xml | 14.4 KB | Display | FSC data file |
| Images | emd_66834.png | 49.6 KB | ||
| Filedesc metadata | emd-66834.cif.gz | 7.3 KB | ||
| Others | emd_66834_half_map_1.map.gz emd_66834_half_map_2.map.gz | 285.8 MB 285.8 MB | ||
| Archive directory | https://data.pdbj.org/pub/emdb/structures/EMD-66834 ftp://data.pdbj.org/pub/emdb/structures/EMD-66834 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9xfoMC ![]() 24glC ![]() 24gtC ![]() 25fqC ![]() 9xbyC ![]() 9xfgC M: atomic model generated by this map C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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| Related items in Molecule of the Month |
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Map
| File | Download / File: emd_66834.map.gz / Format: CCP4 / Size: 307.5 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 0.76 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Half map: #2
| File | emd_66834_half_map_1.map | ||||||||||||
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| Density Histograms |
-Half map: #1
| File | emd_66834_half_map_2.map | ||||||||||||
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| Density Histograms |
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Sample components
-Entire : BAM-SurA complex (P2-visible 1)
| Entire | Name: BAM-SurA complex (P2-visible 1) |
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| Components |
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-Supramolecule #1: BAM-SurA complex (P2-visible 1)
| Supramolecule | Name: BAM-SurA complex (P2-visible 1) / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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-Supramolecule #2: BAM complex
| Supramolecule | Name: BAM complex / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #1-#5 |
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| Source (natural) | Organism: ![]() |
-Supramolecule #3: Chaperone SurA
| Supramolecule | Name: Chaperone SurA / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #6 |
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| Source (natural) | Organism: ![]() |
-Macromolecule #1: Outer membrane protein assembly factor BamA
| Macromolecule | Name: Outer membrane protein assembly factor BamA / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 90.62732 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: MAMKKLLIAS LLFSSATVYG AEGFVVKDIH FEGLQRVAVG AALLSMPVRT GDTVNDEDIS NTIRALFATG NFEDVRVLRD GDTLLVQVK ERPTIASITF SGNKSVKDDM LKQNLEASGV RVGESLDRTT IADIEKGLED FYYSVGKYSA SVKAVVTPLP R NRVDLKLV ...String: MAMKKLLIAS LLFSSATVYG AEGFVVKDIH FEGLQRVAVG AALLSMPVRT GDTVNDEDIS NTIRALFATG NFEDVRVLRD GDTLLVQVK ERPTIASITF SGNKSVKDDM LKQNLEASGV RVGESLDRTT IADIEKGLED FYYSVGKYSA SVKAVVTPLP R NRVDLKLV FQEGVSAEIQ QINIVGNHAF TTDELISHFQ LRDEVPWWNV VGDRKYQKQK LAGDLETLRS YYLDRGYARF NI DSTQVSL TPDKKGIYVT VNITEGDQYK LSGVEVCGNL AGHSAEIEQL TKIEPGELYN GTKVTKMEDD IKKLLGRYGY AYP RVQSMP EINDADKTVK LRVNVDAGNR FYVRKIRFEG NDTSKDAVLR REMRQMEGAW LGSDLVDQGK ERLNRLGFFE TVDT DTQRV PGSPDQVDVV YKVKERNTGS FNFGIGYGTE SGVSFQAGVQ QDNWLGTGYA VGINGTKNDY QTYAELSVTN PYFTV DGVS LGGRLFYNDF QADDADLSDY TNKSYGTDVT LGFPINEYNS LRAGLGYVHN SLSNMQPQVA MWRYLYSMGE HPSTSD QDN SFKTDDFTFN YGWTYNKLDR GYFPTDGSRV NLTGKVTIPG SDNEYYKVTL DTATYVPIDD DHKWVVLGRT RWGYGDG LG GKEMPFYENF YAGGSSTVRG FQSNTIGPKA VYFPHQASNY DPDYDYESAT QDGAKDLSKS DDAVGGNAMA VASLEFIT P TPFISDKYAN SVRTSFFWDM GTVWDTNWDS SQYSGYPDYS DPSNIRMSAG IALQWMSPLG PLVFSYAQPF KKYDGDKAE QFQFNIGKTW UniProtKB: Outer membrane protein assembly factor BamA |
-Macromolecule #2: Outer membrane protein assembly factor BamB
| Macromolecule | Name: Outer membrane protein assembly factor BamB / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 41.918945 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: MQLRKLLLPG LLSVTLLSGC SLFNSEEDVV KMSPLPTVEN QFTPTTAWST SVGSGIGNFY SNLHPALADN VVYAADRAGL VKALNADDG KEIWSVSLAE KDGWFSKEPA LLSGGVTVSG GHVYIGSEKA QVYALNTSDG TVAWQTKVAG EALSRPVVSD G LVLIHTSN ...String: MQLRKLLLPG LLSVTLLSGC SLFNSEEDVV KMSPLPTVEN QFTPTTAWST SVGSGIGNFY SNLHPALADN VVYAADRAGL VKALNADDG KEIWSVSLAE KDGWFSKEPA LLSGGVTVSG GHVYIGSEKA QVYALNTSDG TVAWQTKVAG EALSRPVVSD G LVLIHTSN GQLQALNEAD GAVKWTVNLD MPSLSLRGES APTTAFGAAV VGGDNGRVSA VLMEQGQMIW QQRISQATGS TE IDRLSDV DTTPVVVNGV VFALAYNGNL TALDLRSGQI MWKRELGSVN DFIVDGNRIY LVDQNDRVMA LTIDGGVTLW TQS DLLHRL LTSPVLYNGN LVVGDSEGYL HWINVEDGRF VAQQKVDSSG FQTEPVAADG KLLIQAKDGT VYSITR UniProtKB: Outer membrane protein assembly factor BamB |
-Macromolecule #3: Outer membrane protein assembly factor BamC
| Macromolecule | Name: Outer membrane protein assembly factor BamC / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 36.875277 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: MAYSVQKSRL AKVAGVSLVL LLAACSSDSR YKRQVSGDEA YLEAAPLAEL HAPAGMILPV TSGDYAIPVT NGSGAVGKAL DIRPPAQPL ALVSGARTQF TGDTASLLVE NGRGNTLWPQ VVSVLQAKNY TITQRDDAGQ TLTTDWVQWN RLDEDEQYRG R YQISVKPQ ...String: MAYSVQKSRL AKVAGVSLVL LLAACSSDSR YKRQVSGDEA YLEAAPLAEL HAPAGMILPV TSGDYAIPVT NGSGAVGKAL DIRPPAQPL ALVSGARTQF TGDTASLLVE NGRGNTLWPQ VVSVLQAKNY TITQRDDAGQ TLTTDWVQWN RLDEDEQYRG R YQISVKPQ GYQQAVTVKL LNLEQAGKPV ADAASMQRYS TEMMNVISAG LDKSATDAAN AAQNRASTTM DVQSAADDTG LP MLVVRGP FNVVWQRLPA ALEKVGMKVT DSTRSQGNMA VTYKPLSDSD WQELGASDPG LASGDYKLQV GDLDNRSSLQ FID PKGHTL TQSQNDALVA VFQAAFSK UniProtKB: Outer membrane protein assembly factor BamC |
-Macromolecule #4: Outer membrane protein assembly factor BamD
| Macromolecule | Name: Outer membrane protein assembly factor BamD / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 27.85835 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: MTRMKYLVAA ATLSLFLAGC SGSKEEVPDN PPNEIYATAQ QKLQDGNWRQ AITQLEALDN RYPFGPYSQQ VQLDLIYAYY KNADLPLAQ AAIDRFIRLN PTHPNIDYVM YMRGLTNMAL DDSALQGFFG VDRSDRDPQH ARAAFSDFSK LVRGYPNSQY T TDATKRLV ...String: MTRMKYLVAA ATLSLFLAGC SGSKEEVPDN PPNEIYATAQ QKLQDGNWRQ AITQLEALDN RYPFGPYSQQ VQLDLIYAYY KNADLPLAQ AAIDRFIRLN PTHPNIDYVM YMRGLTNMAL DDSALQGFFG VDRSDRDPQH ARAAFSDFSK LVRGYPNSQY T TDATKRLV FLKDRLAKYE YSVAEYYTER GAWVAVVNRV EGMLRDYPDT QATRDALPLM ENAYRQMQMN AQAEKVAKII AA NSSNT UniProtKB: Outer membrane protein assembly factor BamD |
-Macromolecule #5: Outer membrane protein assembly factor BamE
| Macromolecule | Name: Outer membrane protein assembly factor BamE / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 12.310977 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: MRCKTLTAAA AVLLMLTAGC STLERVVYRP DINQGNYLTA NDVSKIRVGM TQQQVAYALG TPLMSDPFGT NTWFYVFRQQ PGHEGVTQQ TLTLTFNSSG VLTNIDNKPA LSGN UniProtKB: Outer membrane protein assembly factor BamE |
-Macromolecule #6: Chaperone SurA
| Macromolecule | Name: Chaperone SurA / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO / EC number: peptidylprolyl isomerase |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 48.781176 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: MAKNWKTLLL GIAMIANTSF AAPQVVDKVA AVVNNGVVLE SDVDGLMQSV KLNAAQARQQ LPDDATLRHQ IMERLIMDQI ILQMGQKMG VKISDEQLDQ AIANIAKQNN MTLDQMRSRL AYDGLNYNTY RNQIRKEMII SEVRNNEVRR RITILPQEVE S LAQQVGNQ ...String: MAKNWKTLLL GIAMIANTSF AAPQVVDKVA AVVNNGVVLE SDVDGLMQSV KLNAAQARQQ LPDDATLRHQ IMERLIMDQI ILQMGQKMG VKISDEQLDQ AIANIAKQNN MTLDQMRSRL AYDGLNYNTY RNQIRKEMII SEVRNNEVRR RITILPQEVE S LAQQVGNQ NDASTELNLS HILIPLPENP TSDQVNEAES QARAIVDQAR NGADFGKLAI AHSADQQALN GGQMGWGRIQ EL PGIFAQA LSTAKKGDIV GPIRSGVGFH ILKVNDLRGE SKNISVTEVH ARHILLKPSP IMTDEQARVK LEQIAADIKS GKT TFAAAA KEFSQDPGSA CQGGDLGWAT PDIFDPAFRD ALTRLNKGQM SAPVHSSFGW HLIELLDTRN VDKTDAAQKD RAYR MLMNR KFSEEAASWM QEQRASAYVK ILSNHHHHHH HHHH UniProtKB: Chaperone SurA |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Buffer | pH: 8 |
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| Vitrification | Cryogen name: ETHANE |
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Electron microscopy
| Microscope | TFS KRIOS |
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| Image recording | Film or detector model: TFS FALCON 4i (4k x 4k) / Average electron dose: 30.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.6 µm / Nominal defocus min: 0.6 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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About Yorodumi




Keywords
Authors
Japan, 1 items
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Processing
FIELD EMISSION GUN

