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- EMDB-44793: E. coli cellulose synthase BcsAG3B6 complex - Consensus map -

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Basic information

Entry
Database: EMDB / ID: EMD-44793
TitleE. coli cellulose synthase BcsAG3B6 complex - Consensus map
Map dataLow resolution consensus map
Sample
  • Complex: Bacterial cellulose synthase BcsA-BcsG3-BcsB6 complex
    • Protein or peptide: Bacterial cellulose synthase subunit A (BcsA)
    • Protein or peptide: Bacterial cellulose synthase subunit B (BcsB)
    • Protein or peptide: Bacterial cellulose synthase subunit G (BcsG)
Keywordsphosphoethanolamine (pEtN) / catalytic BcsA-B / c-di-GMP binding protein / membrane proteins / TRANSFERASE
Biological speciesEscherichia coli (E. coli)
Methodsingle particle reconstruction / cryo EM / Resolution: 5.67 Å
AuthorsVerma P / Zimmer J
Funding support United States, 1 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)R35GM144130 United States
CitationJournal: Nat Commun / Year: 2024
Title: Insights into phosphoethanolamine cellulose synthesis and secretion across the Gram-negative cell envelope.
Authors: Preeti Verma / Ruoya Ho / Schuyler A Chambers / Lynette Cegelski / Jochen Zimmer /
Abstract: Phosphoethanolamine (pEtN) cellulose is a naturally occurring modified cellulose produced by several Enterobacteriaceae. The minimal components of the E. coli cellulose synthase complex include the ...Phosphoethanolamine (pEtN) cellulose is a naturally occurring modified cellulose produced by several Enterobacteriaceae. The minimal components of the E. coli cellulose synthase complex include the catalytically active BcsA enzyme, a hexameric semicircle of the periplasmic BcsB protein, and the outer membrane (OM)-integrated BcsC subunit containing periplasmic tetratricopeptide repeats (TPR). Additional subunits include BcsG, a membrane-anchored periplasmic pEtN transferase associated with BcsA, and BcsZ, a periplasmic cellulase of unknown biological function. While cellulose synthesis and translocation by BcsA are well described, little is known about its pEtN modification and translocation across the cell envelope. We show that the N-terminal cytosolic domain of BcsA positions three BcsG copies near the nascent cellulose polymer. Further, the semicircle's terminal BcsB subunit tethers the N-terminus of a single BcsC protein in a trans-envelope secretion system. BcsC's TPR motifs bind a putative cello-oligosaccharide near the entrance to its OM pore. Additionally, we show that only the hydrolytic activity of BcsZ but not the subunit itself is necessary for cellulose secretion, suggesting a secretion mechanism based on enzymatic removal of translocation incompetent cellulose. Lastly, protein engineering introduces cellulose pEtN modification in orthogonal cellulose biosynthetic systems. These findings advance our understanding of pEtN cellulose modification and secretion.
History
DepositionMay 8, 2024-
Header (metadata) releaseFeb 19, 2025-
Map releaseFeb 19, 2025-
UpdateFeb 19, 2025-
Current statusFeb 19, 2025Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_44793.png

Downloads & links

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Map

FileDownload / File: emd_44793.map.gz / Format: CCP4 / Size: 178 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationLow resolution consensus map
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.08 Å/pix.
x 360 pix.
= 388.8 Å		1.08 Å/pix.
x 360 pix.
= 388.8 Å		1.08 Å/pix.
x 360 pix.
= 388.8 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.08 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.12
Minimum - Maximum-0.5806579 - 1.0829483
Average (Standard dev.)0.000990627 (±0.034742586)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions360360360
Spacing360360360
CellA=B=C: 388.80002 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: Half map A

Fileemd_44793_half_map_1.map
AnnotationHalf map A
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Half map B

Fileemd_44793_half_map_2.map
AnnotationHalf 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 : Bacterial cellulose synthase BcsA-BcsG3-BcsB6 complex

EntireName: Bacterial cellulose synthase BcsA-BcsG3-BcsB6 complex
Components
  • Complex: Bacterial cellulose synthase BcsA-BcsG3-BcsB6 complex
    • Protein or peptide: Bacterial cellulose synthase subunit A (BcsA)
    • Protein or peptide: Bacterial cellulose synthase subunit B (BcsB)
    • Protein or peptide: Bacterial cellulose synthase subunit G (BcsG)

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Supramolecule #1: Bacterial cellulose synthase BcsA-BcsG3-BcsB6 complex

SupramoleculeName: Bacterial cellulose synthase BcsA-BcsG3-BcsB6 complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Details: Proteins: 1. Bacterial cellulose synthase subunit A (BcsA) 2. Bacterial cellulose synthase subunit B (BcsB) 3. Bacterial cellulose synthase subunit G (BcsG)
Source (natural)Organism: Escherichia coli (E. coli)

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Macromolecule #1: Bacterial cellulose synthase subunit A (BcsA)

MacromoleculeName: Bacterial cellulose synthase subunit A (BcsA) / type: protein_or_peptide / ID: 1 / Enantiomer: LEVO
Source (natural)Organism: Escherichia coli (E. coli)
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: mgsiltrwll ippvnarlig ryrdyrrhga safsatlgcf wmilawifip lehprwqrir aehknlyph inasrprpld pvryliqtcw lligasrket pkprrrafsg lqnirgryhq w mnelperv shktqhldek kelghlsaga rrlilgiivt fslilalicv ...String:
mgsiltrwll ippvnarlig ryrdyrrhga safsatlgcf wmilawifip lehprwqrir aehknlyph inasrprpld pvryliqtcw lligasrket pkprrrafsg lqnirgryhq w mnelperv shktqhldek kelghlsaga rrlilgiivt fslilalicv tqpfnplaqf if lmllwgv alivrrmpgr fsalmlivls ltvscryiww rytstlnwdd pvslvcglil lfa etyawi vlvlgyfqvv wplnrqpvpl pkdmslwpsv difvptyned lnvvkntiya slgi dwpkd klniwilddg greefrqfaq nvgvkyiart thehakagni nnalkyakge fvsif dcdh vptrsflqmt mgwflkekql ammqtphhff spdpfernlg rfrktpnegt lfyglv qdg ndmwdatffc gscavirrkp ldeiggiave tvtedahtsl rlhrrgytsa ymripqa ag lateslsahi gqrirwargm vqifrldnpl tgkglkfaqr lcyvnamfhf lsgiprli f ltaplaflll hayiiyapal mialfvlphm ihasltnski qgkyrhsfws eiyetvlaw yiapptlval inphkgkfnv takgglveee yvdwvisrpy iflvllnlvg vavgiwryfy gpptemltv vvsmvwvfyn livlggavav sveskqvrrs hrvemtmpaa iaredghlfs c tvqdfsdg glgikingqa qilegqkvnl llkrgqqeyv fptqvarvmg nevglklmpl tt qqhidfv qctfaradtw alwqdsyped kpleslldil klgfrgyrhl aefapssvkg ifr vltslv swvvsfiprr persetaqps dqalaqqHHH HHHLEHHHHH H

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Macromolecule #2: Bacterial cellulose synthase subunit B (BcsB)

MacromoleculeName: Bacterial cellulose synthase subunit B (BcsB) / type: protein_or_peptide / ID: 2 / Enantiomer: LEVO
Source (natural)Organism: Escherichia coli (E. coli)
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: AWSHPQFEKt patqplinae pavaaqteqn pqvgq vmpg vqgadapvva qngpsrdvkl tfaqiapppg smvlrginpn gsiefgmrsd evvtka mln leytpspsll pvqsqlkvyl ndelmgvlpv tkeqlgkktl aqmpinplfi sdfnrvr le fvghyqdvce ...String:
AWSHPQFEKt patqplinae pavaaqteqn pqvgq vmpg vqgadapvva qngpsrdvkl tfaqiapppg smvlrginpn gsiefgmrsd evvtka mln leytpspsll pvqsqlkvyl ndelmgvlpv tkeqlgkktl aqmpinplfi sdfnrvr le fvghyqdvce kpasttlwld vgrssgldlt yqtlnvkndl shfpvpffdp sdnrtntl p mvfagapdvg lqqasaivas wfgsrsgwrg qnfpvlynql pdrnaivfat ndkrpdflr dhpavkapvi eminhpqnpy vkllvvfgrd dkdllqaakg iaqgnilfrg esvvvnevkp llprkpyda pnwvrtdrpv tfgelktyee qlqssglepa ainvslnlpp dlylmrstgi d mdinyryt mppvkdssrm dislnnqflq sfnlsskqea nrlllripvl qglldgktdv si palklga tnqlrfdfey mnpmpggsvd ncitfqpvqn hvvigddsti dfskyyhfip mpd lrafan agfpfsrmad lsqtitvmpk apneaqmetl lntvgfigaq tgfpainltv tddg stiqg kdadimiigg ipdklkddkq idllvqates wvktpmrqtp fpgivpdesd raaet rstl tssgamaavi gfqspyndqr svialladsp rgyemlndav ndsgkratmf gsvavi res ginslrvgdv yyvghlpwfe rvwyalanhp illavlaais villawvlwr llriisr rr lnpdne

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Macromolecule #3: Bacterial cellulose synthase subunit G (BcsG)

MacromoleculeName: Bacterial cellulose synthase subunit G (BcsG) / type: protein_or_peptide / ID: 3 / Enantiomer: LEVO
Source (natural)Organism: Escherichia coli (E. coli)
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MTQFTQNTAM PSSLWQYWRG LSGWNFYFLV KFGLLWAGYL NFHPLLNLVF AAFLLMPLPR YSLHRLRHW IALPIGFALF WHDTWLPGPE SIMSQGSQVA GFSTDYLIDL VTRFINWQMI G AIFVLLVA WLFLSQWIRI TVFVVAILLW LNVLTLAGPS FSLWPAGQPT ...String:
MTQFTQNTAM PSSLWQYWRG LSGWNFYFLV KFGLLWAGYL NFHPLLNLVF AAFLLMPLPR YSLHRLRHW IALPIGFALF WHDTWLPGPE SIMSQGSQVA GFSTDYLIDL VTRFINWQMI G AIFVLLVA WLFLSQWIRI TVFVVAILLW LNVLTLAGPS FSLWPAGQPT TTVTTTGGNA AA TVAATGG APVVGDMPAQ TAPPTTANLN AWLNNFYNAE AKRKSTFPSS LPADAQPFEL LVI NICSLS WSDIEAAGLM SHPLWSHFDI EFKNFNSATS YSGPAAIRLL RASCGQTSHT NLYQ PANND CYLFDNLSKL GFTQHLMMGH NGQFGGFLKE VRENGGMQSE LMDQTNLPVI LLGFD GSPV YDDTAVLNRW LDVTEKDKNS RSATFYNTLP LHDGNHYPGV SKTADYKARA QKFFDE LDA FFTELEKSGR KVMVVVVPEH GGALKGDRMQ VSGLRDIPSP SITDVPVGVK FFGMKAP HQ GAPIVIEQPS SFLAISDLVV RVLDGKIFTE DNVDWKKLTS GLPQTAPVSE NSNAVVIQ Y QDKPYVRLNG GDWVPYPQDY KDDDDK

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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

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 51.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.5 µm / Nominal defocus min: 1.0 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup model#0 - Type of model: INSILICO MODEL / #0 - In silico model: AlphaFold2 model of BcsA-BcsG3 / #1 - Type of model: PDB ENTRY
#1 - PDB model - PDB ID:

7l2z


#1 - Details: PDB: 7L2Z for BcsB hexamer
Final reconstructionResolution.type: BY AUTHOR / Resolution: 5.67 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 39522
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
FSC plot (resolution estimation)

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