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- EMDB-16073: Full-length bacterial polysaccharide co-polymerase WzzE from E. c... -
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Open data
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Basic information
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Title | Full-length bacterial polysaccharide co-polymerase WzzE from E. coli. C8 symmetry | ||||||||||||
![]() | C8 symmetrized map of the E. coli polysaccharide co-polymerase WzzE | ||||||||||||
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![]() | Complex / Lipopolysaccharide / bacterial polysaccharide co-polymerase / MEMBRANE PROTEIN | ||||||||||||
Function / homology | ECA polysaccharide chain length modulation protein WzzE / enterobacterial common antigen biosynthetic process / : / Polysaccharide chain length determinant N-terminal domain / Chain length determinant protein / protein tyrosine kinase activity / plasma membrane / ECA polysaccharide chain length modulation protein![]() | ||||||||||||
Biological species | ![]() ![]() | ||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.1 Å | ||||||||||||
![]() | Wiseman B / Hogbom M | ||||||||||||
Funding support | ![]()
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![]() | ![]() Title: Alternating L4 loop architecture of the bacterial polysaccharide co-polymerase WzzE. Authors: Benjamin Wiseman / Göran Widmalm / Martin Högbom / ![]() Abstract: Lipopolysaccharides such as the enterobacterial common antigen are important components of the enterobacterial cell envelope that act as a protective barrier against the environment and are often ...Lipopolysaccharides such as the enterobacterial common antigen are important components of the enterobacterial cell envelope that act as a protective barrier against the environment and are often polymerized by the inner membrane bound Wzy-dependent pathway. By employing cryo-electron microscopy we show that WzzE, the co-polymerase component of this pathway that is responsible for the length modulation of the enterobacterial common antigen, is octameric with alternating up-down conformations of its L4 loops. The alternating up-down nature of these essential loops, located at the top of the periplasmic bell, are modulated by clashing helical faces between adjacent protomers that flank the L4 loops around the octameric periplasmic bell. This alternating arrangement and a highly negatively charged binding face create a dynamic environment in which the polysaccharide chain is extended, and suggest a ratchet-type mechanism for polysaccharide elongation. | ||||||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 120.8 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 17.2 KB 17.2 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 15.6 KB | Display | ![]() |
Images | ![]() | 88.3 KB | ||
Others | ![]() ![]() | 226.4 MB 226.4 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8bhwC ![]() 8p3oC ![]() 8p3pC C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Map
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Annotation | C8 symmetrized map of the E. coli polysaccharide co-polymerase WzzE | ||||||||||||||||||||
Voxel size | X=Y=Z: 1.06 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: Half map A for C8 symmetrized map of...
File | emd_16073_half_map_1.map | ||||||||||||
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Annotation | Half map A for C8 symmetrized map of the E. coli polysaccharide co-polymerase WzzE | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Half map B for C8 symmetrized map of...
File | emd_16073_half_map_2.map | ||||||||||||
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Annotation | Half map B for C8 symmetrized map of the E. coli polysaccharide co-polymerase WzzE | ||||||||||||
Projections & Slices |
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Density Histograms |
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Sample components
-Entire : Bacterial Polysaccharide Co-polymerase WzzE
Entire | Name: Bacterial Polysaccharide Co-polymerase WzzE |
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Components |
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-Supramolecule #1: Bacterial Polysaccharide Co-polymerase WzzE
Supramolecule | Name: Bacterial Polysaccharide Co-polymerase WzzE / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all / Details: Homo octameric complex |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 320 KDa |
-Macromolecule #1: polysaccharide co-polymerase WzzE
Macromolecule | Name: polysaccharide co-polymerase WzzE / type: protein_or_peptide / ID: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MTQPMPGKPA EDAENELDIR GLFRTLWAGK LWIIGMGLAF ALIALAYTFF ARQEWSSTAI TDRPTVNMLG GYYSQQQFLR NLDVRSNMA SADQPSVMDE AYKEFVMQLA SWDTRREFWL QTDYYKQRMV GNSKADAALL DEMINNIQFI PGDFTRAVND S VKLIAETA ...String: MTQPMPGKPA EDAENELDIR GLFRTLWAGK LWIIGMGLAF ALIALAYTFF ARQEWSSTAI TDRPTVNMLG GYYSQQQFLR NLDVRSNMA SADQPSVMDE AYKEFVMQLA SWDTRREFWL QTDYYKQRMV GNSKADAALL DEMINNIQFI PGDFTRAVND S VKLIAETA PDANNLLRQY VAFASQRAAS HLNDELKGAW AARTIQMKAQ VKRQEEVAKA IYDRRMNSIE QALKIAEQHN IS RSATDVP AEELPDSEMF LLGRPMLQAR LENLQAVGPA FDLDYDQNRA MLNTLNVGPT LDPRFQTYRY LRTPEEPVKR DSP RRAFLM IMWGIVGGLI GAGVALTRRC SKEFRVPGSH HHHHHHH UniProtKB: ECA polysaccharide chain length modulation protein |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Concentration | 3.0 mg/mL |
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Buffer | pH: 8 |
Grid | Model: C-flat-2/2 / Material: GOLD / Mesh: 300 / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 40 sec. / Pretreatment - Atmosphere: AIR |
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: COUNTING / Digitization - Frames/image: 1-40 / Number grids imaged: 1 / Number real images: 5111 / Average electron dose: 52.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 3.2 µm / Nominal defocus min: 1.4000000000000001 µm |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |