|Entry||Database: EMDB / ID: 3611|
|Title||Full-length dodecameric S. typhimurium Wzz complex with associated dodecyl maltoside micelle.|
|Map data||Wzz dodecamer with dodecyl maltoside micelle|
|Source||Staphylococcus aureus / / bacteria|
|Method||single particle reconstruction / cryo EM / 9 Å resolution|
|Authors||Ford RC / Kargas V|
|Citation||Journal: Structure / Year: 2017|
Title: Full-length, Oligomeric Structure of Wzz Determined by Cryoelectron Microscopy Reveals Insights into Membrane-Bound States.
Authors: Richard F Collins / Vasileios Kargas / Brad R Clarke / C Alistair Siebert / Daniel K Clare / Peter J Bond / Chris Whitfield / Robert C Ford
Abstract: Wzz is an integral inner membrane protein involved in regulating the length of lipopolysaccharide O-antigen glycans and essential for the virulence of many Gram-negative pathogens. In all Wzz ...Wzz is an integral inner membrane protein involved in regulating the length of lipopolysaccharide O-antigen glycans and essential for the virulence of many Gram-negative pathogens. In all Wzz homologs, the large periplasmic domain is proposed to be anchored by two transmembrane helices, but no information is available for the transmembrane and cytosolic domains. Here we have studied purified oligomeric Wzz complexes using cryoelectron microscopy and resolved the transmembrane regions within a semi-continuous detergent micelle. The transmembrane helices of each monomer display a right-handed super-helical twist, and do not interact with the neighboring transmembrane domains. Modeling, flexible fitting and multiscale simulation approaches were used to study the full-length complex and to provide explanations for the influence of the lipid bilayer on its oligomeric status. Based on structural and in silico observations, we propose a new mechanism for O-antigen chain-length regulation that invokes synergy of Wzz and its polymerase partner, Wzy.
Copyright: 2017 Elsevier Ltd. All rights reserved.
|Validation Report||PDB-ID: 5nbz|
SummaryFull reportAbout validation report
|Date||Deposition: Mar 2, 2017 / Header (metadata) release: Apr 5, 2017 / Map release: Apr 5, 2017 / Last update: Jun 28, 2017|
|Structure viewer||EM map: |
Downloads & links
|File||emd_3611.map.gz (map file in CCP4 format, 67109 KB)|
|Projections & slices|
Images are generated by Spider.
|Voxel size||X=Y=Z: 1.45 Å|
CCP4 map header:
-Entire Dodecameric complex
|Entire||Name: Dodecameric complex / Number of components: 2|
|Mass||Theoretical: 360 kDa|
-Component #1: protein, Dodecameric complex
|Protein||Name: Dodecameric complex / Recombinant expression: No|
|Mass||Theoretical: 360 kDa|
|Source||Species: Staphylococcus aureus / / bacteria|
|Source (engineered)||Expression System: Escherichia coli / / bacteria /|
-Component #2: protein, WzzB
|Protein||Name: WzzB / Recombinant expression: No|
|Mass||Theoretical: 26.760129 kDa|
|Source (engineered)||Expression System: Staphylococcus aureus / / bacteria|
|Specimen||Specimen state: particle / Method: cryo EM|
|Sample solution||Specimen conc.: 0.3 mg/ml|
Buffer solution: 20mM Tris pH 7.5, 150mM NaCl, 0.025% dodecyl maltoside.
|Vitrification||Instrument: FEI VITROBOT MARK III / Cryogen name: ETHANE / Temperature: 293 K / Humidity: 95 % / Details: 1 x 4sec blot|
-Electron microscopy imaging
Model: Titan Krios / Image courtesy: FEI Company
|Imaging||Microscope: FEI TITAN KRIOS|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Electron dose: 2 e/Å2 / Illumination mode: FLOOD BEAM|
|Lens||Imaging mode: BRIGHT FIELD|
|Specimen Holder||Model: FEI TITAN KRIOS AUTOGRID HOLDER|
|Camera||Detector: GATAN K2 (4k x 4k)|
|Processing||Method: single particle reconstruction / Number of projections: 22000|
|3D reconstruction||Resolution: 9 Å / Resolution method: OTHER / Details: ResMap|
-Atomic model buiding
|Modeling #1||Refinement protocol: flexible / Refinement space: REAL / Input PDB model: 4E29|
Chain ID: 4E29_A
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