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- PDB-26gs: Colanic acid polysaccharide related protein structures -

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Basic information

Entry
Database: PDB / ID: 26gs
TitleColanic acid polysaccharide related protein structures
Components
  • Putative polysaccharide export protein Wza
  • Tyrosine-protein kinase wzc
KeywordsPROTEIN TRANSPORT / Complex
Function / homology
Function and homology information


colanic acid metabolic process / Transferases; Transferring phosphorus-containing groups; Protein-tyrosine kinases / polysaccharide transmembrane transporter activity / colanic acid biosynthetic process / polysaccharide transport / polysaccharide biosynthetic process / peptidyl-tyrosine autophosphorylation / porin activity / pore complex / monoatomic ion transport ...colanic acid metabolic process / Transferases; Transferring phosphorus-containing groups; Protein-tyrosine kinases / polysaccharide transmembrane transporter activity / colanic acid biosynthetic process / polysaccharide transport / polysaccharide biosynthetic process / peptidyl-tyrosine autophosphorylation / porin activity / pore complex / monoatomic ion transport / cell outer membrane / protein tyrosine kinase activity / ATP hydrolysis activity / ATP binding / identical protein binding / plasma membrane
Similarity search - Function
Outer-membrane lipoprotein Wza, C-terminal domain / Outer-membrane lipoprotein Wza C-terminal domain / Polysaccharide export protein / : / Polysaccharide biosynthesis/export protein / Tyrosine-protein kinase Wzc, N-terminal domain / Tyrosine kinase, G-rich domain / G-rich domain on putative tyrosine kinase / Exopolysaccharide synthesis protein / Polysaccharide chain length determinant N-terminal domain ...Outer-membrane lipoprotein Wza, C-terminal domain / Outer-membrane lipoprotein Wza C-terminal domain / Polysaccharide export protein / : / Polysaccharide biosynthesis/export protein / Tyrosine-protein kinase Wzc, N-terminal domain / Tyrosine kinase, G-rich domain / G-rich domain on putative tyrosine kinase / Exopolysaccharide synthesis protein / Polysaccharide chain length determinant N-terminal domain / Chain length determinant protein / AAA domain / AAA domain / : / : / SLBB domain / Prokaryotic membrane lipoprotein lipid attachment site profile. / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
Putative polysaccharide export protein Wza / Tyrosine-protein kinase wzc
Similarity search - Component
Biological speciesEscherichia coli K-12 (bacteria)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3 Å
Authorsjiao, L. / Yanlong, H.
Funding support China, 1items
OrganizationGrant numberCountry
Chinese Academy of Sciences China
CitationJournal: Nat Commun / Year: 2026
Title: Architecture of the Wza-Wzc complex that mediates colanic acid translocation across the cell envelope in Gram-negative bacteria.
Authors: Jiao Liu / Yanlong Han / Guanxue Huang / Manfeng Zhang / Junlei Du / Haizhen Zhou / Dahua Chen / Yihua Huang /
Abstract: The Wzx/Wzy-dependent pathway is a highly conserved mechanism for bacterial polysaccharide biosynthesis. This pathway is exemplified by the assembly and export of colanic acid mediated by the Wza-Wzc ...The Wzx/Wzy-dependent pathway is a highly conserved mechanism for bacterial polysaccharide biosynthesis. This pathway is exemplified by the assembly and export of colanic acid mediated by the Wza-Wzc complex. While recent structural investigations have yielded valuable insights into the molecular basis of colanic acid biosynthesis, the overall architecture of the Wza-Wzc complex and the regulatory mechanism of colanic acid export remain incompletely understood. Here, we report cryo-electron microscopy (cryo-EM) structures of the Wza-Wzc complex from E. coli K12 in two functionally states: the autophosphorylated wild-type (Wza-Wzc) state and the non-phosphorylated (Wza-Wzc) state. Both structures reveal that Wza and Wzc assemble into a continuous channel spanning the entire bacterial cell envelope, indicating that phosphorylation of Wzc does not disassemble the intact export channel. Relative to Wza-Wzc, the octameric periplasmic domain of Wzc in Wza-Wzc undergoes a significant conformational rearrangement. This rearrangement reduces constriction region's diameter and confers a negatively charged property to the interior of the Wzc octamer, which is proposed to inhibit colanic acid export. Collectively, these structural findings confirm that the Wza-Wzc complex forms a colanic acid export channel throughout Wzc's phosphorylation-dephosphorylation cycle, advancing our mechanistic understanding of the Wzx/Wzy-dependent polysaccharide biosynthesis pathway in Gram-negative bacteria.
History
DepositionApr 29, 2026Deposition site: PDBJ / Processing site: PDBC
Revision 1.0Jun 24, 2026Provider: repository / Type: Initial release
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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Tyrosine-protein kinase wzc
O: Putative polysaccharide export protein Wza
B: Tyrosine-protein kinase wzc
C: Putative polysaccharide export protein Wza
D: Tyrosine-protein kinase wzc
E: Putative polysaccharide export protein Wza
F: Tyrosine-protein kinase wzc
G: Putative polysaccharide export protein Wza
H: Tyrosine-protein kinase wzc
I: Putative polysaccharide export protein Wza
J: Tyrosine-protein kinase wzc
K: Putative polysaccharide export protein Wza
L: Tyrosine-protein kinase wzc
M: Putative polysaccharide export protein Wza
N: Tyrosine-protein kinase wzc
P: Putative polysaccharide export protein Wza


Theoretical massNumber of molelcules
Total (without water)659,20916
Polymers659,20916
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: electron microscopy, not applicable
TypeNameSymmetry operationNumber
identity operation1_5551

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Components

#1: Protein
Tyrosine-protein kinase wzc


Mass: 42644.277 Da / Num. of mol.: 8
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli K-12 (bacteria) / Gene: wzc, b2060, JW2045 / Production host: Escherichia coli (E. coli)
References: UniProt: P76387, Transferases; Transferring phosphorus-containing groups; Protein-tyrosine kinases
#2: Protein
Putative polysaccharide export protein Wza


Mass: 39756.898 Da / Num. of mol.: 8
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli K-12 (bacteria) / Gene: wza, b2062, JW2047 / Production host: Escherichia coli (E. coli) / References: UniProt: P0A930
Has protein modificationN

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: Wza-Wzc complex / Type: COMPLEX / Entity ID: all / Source: RECOMBINANT
Source (natural)Organism: Escherichia coli K-12 (bacteria)
Source (recombinant)Organism: Escherichia coli (E. coli)
Buffer solutionpH: 8
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationCryogen name: NITROGEN

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Electron microscopy imaging

MicroscopyModel: TFS TALOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal defocus max: 2000 nm / Nominal defocus min: 1200 nm
Image recordingElectron dose: 60 e/Å2 / Film or detector model: GATAN K3 (6k x 4k)

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Processing

EM software
IDNameVersionCategory
1cryoSPARCparticle selection
2PHENIX1.20.1_4487model refinement
13cryoSPARC3D reconstruction
CTF correctionType: PHASE FLIPPING ONLY
3D reconstructionResolution: 3 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 16148 / Symmetry type: POINT
RefinementHighest resolution: 3 Å
Stereochemistry target values: REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS)
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.0146960
ELECTRON MICROSCOPYf_angle_d1.27563712
ELECTRON MICROSCOPYf_dihedral_angle_d6.9566237
ELECTRON MICROSCOPYf_chiral_restr0.0647408
ELECTRON MICROSCOPYf_plane_restr0.018352

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