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Open data
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Basic information
Entry | ![]() | |||||||||
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Title | Wzc-K540M-3YE-N711Y MgADP C1 | |||||||||
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![]() | Wzc-K540M-3YE-N711Y / MEMBRANE PROTEIN | |||||||||
Function / homology | ![]() | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.71 Å | |||||||||
![]() | Liu JW / Yang Y / Naismith JH | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Molecular basis for the phosphorylation of bacterial tyrosine kinase Wzc. Authors: Yun Yang / Mariana Batista / Bradley R Clarke / Michelle R Agyare-Tabbi / Haigang Song / Noah M Kuehfuss / Audrey Le Bas / Carol V Robinson / Chris Whitfield / Phillip J Stansfeld / James H ...Authors: Yun Yang / Mariana Batista / Bradley R Clarke / Michelle R Agyare-Tabbi / Haigang Song / Noah M Kuehfuss / Audrey Le Bas / Carol V Robinson / Chris Whitfield / Phillip J Stansfeld / James H Naismith / Jiwei Liu / ![]() ![]() ![]() Abstract: The regulation of polymerisation and translocation of biomolecules is fundamental. Wzc, an integral cytoplasmic membrane tyrosine autokinase protein serves as the master regulator of the biosynthesis ...The regulation of polymerisation and translocation of biomolecules is fundamental. Wzc, an integral cytoplasmic membrane tyrosine autokinase protein serves as the master regulator of the biosynthesis and export of many bacterial capsular polysaccharides and exopolysaccharides. Such polysaccharides play essential roles in infection, defence, and some are important industrial products. Wzc comprises a large periplasmic domain, two transmembrane helices and a C-terminal cytoplasmic kinase domain with a tyrosine-rich tail. Wzc regulates polymerisation functions through cycling the formation and dissociation of an octameric complex, driven by changes in the phosphorylation status of the tyrosine-rich tail. E. coli Wzc serves a model for a wider family of polysaccharide co-polymerases. Here, we determine structures of intermediate states with different extents of phosphorylation. Structural and computational data reveal the pre-ordering of the tyrosine-rich tail, the molecular basis underlying the unidirectionality of phosphorylation events, and the underlying structural dynamics on how phosphorylation status is transmitted. | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 21.5 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 17.1 KB 17.1 KB | Display Display | ![]() |
Images | ![]() | 109.5 KB | ||
Filedesc metadata | ![]() | 6 KB | ||
Others | ![]() ![]() | 188.4 MB 188.4 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9exqMC ![]() 9exoC ![]() 9expC ![]() 9exrC ![]() 9i2qC ![]() 9i2rC M: atomic model generated by this map 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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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 0.737 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #1
File | emd_50046_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #2
File | emd_50046_half_map_2.map | ||||||||||||
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Density Histograms |
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Sample components
-Entire : Wzc-K540M-3YE-N711Y
Entire | Name: Wzc-K540M-3YE-N711Y |
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Components |
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-Supramolecule #1: Wzc-K540M-3YE-N711Y
Supramolecule | Name: Wzc-K540M-3YE-N711Y / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1 |
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Source (natural) | Organism: ![]() ![]() |
-Macromolecule #1: Putative transmembrane protein Wzc
Macromolecule | Name: Putative transmembrane protein Wzc / type: protein_or_peptide / ID: 1 / Number of copies: 8 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 80.518234 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MTSVTSKQST ILGSDEIDLG RVIGELIDHR KLIISITSVF TLFAILYALL ATPIYETDAL IQIEQKQGNA ILSSLSQVLP DGQPQSAPE TALLQSRMIL GKTIDDLNLQ IQIEQKYFPV IGRGLARLMG EKPGNIDITR LYLPDSDDIS NNTPSIILTV K DKENYSIN ...String: MTSVTSKQST ILGSDEIDLG RVIGELIDHR KLIISITSVF TLFAILYALL ATPIYETDAL IQIEQKQGNA ILSSLSQVLP DGQPQSAPE TALLQSRMIL GKTIDDLNLQ IQIEQKYFPV IGRGLARLMG EKPGNIDITR LYLPDSDDIS NNTPSIILTV K DKENYSIN SDGIQLNGVV GTLLNEKGIS LLVNEIDAKP GDQFVITQLP RLKAISDLLK SFSVADLGKD TGMLTLTLTG DN PKRISHI LDSISQNYLA QNIARQAAQD AKSLEFLNQQ LPKVRAELDS AEDKLNAYRK QKDSVDLNME AKSVLDQIVN VDN QLNELT FREAEVSQLY TKEHPTYKAL MEKRQTLQEE KSKLNKRVSS MPSTQQEVLR LSRDVESGRA VYLQLLNRQQ ELNI AKSSA IGNVRIIDNA VTDPNPVRPK KTIIIVIGVV LGLIVSVVLV LFQVFLRRGI ESPEQLEEIG INVYASIPIS EWLTK NARQ SGKVRKNQSD TLLAVGNPAD LAVEAIRGLR TSLHFAMMEA KNNVLMISGA SPSAGMTFIS SNLAATIAIT GKKVLF IDA DLRKGYAHKM FGHKNDKGLS EFLSGQAAAE MIIDKVEGGG FDYIGRGQIP PNPAELLMHP RFEQLLNWAS QNYDLII ID TPPILAVTDA AIIGRYAGTC LLVARFEKNT VKEIDVSMKR FEQSGVVVKG CILNGVVKKA SSYYRYGHYH YGESEEDK K HHHHHH UniProtKB: Putative transmembrane protein Wzc |
-Macromolecule #2: ADENOSINE-5'-DIPHOSPHATE
Macromolecule | Name: ADENOSINE-5'-DIPHOSPHATE / type: ligand / ID: 2 / Number of copies: 8 / Formula: ADP |
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Molecular weight | Theoretical: 427.201 Da |
Chemical component information | ![]() ChemComp-ADP: |
-Macromolecule #3: MAGNESIUM ION
Macromolecule | Name: MAGNESIUM ION / type: ligand / ID: 3 / Number of copies: 8 / Formula: MG |
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Molecular weight | Theoretical: 24.305 Da |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 7.3 |
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Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 31.9 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.4 µm / Nominal defocus min: 0.8 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
Startup model | Type of model: NONE |
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Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 2.71 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 413751 |
Initial angle assignment | Type: NOT APPLICABLE |
Final angle assignment | Type: NOT APPLICABLE |