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Yorodumi- PDB-8jyx: Crystal structure of the gasdermin-like protein RCD-1-1 from Neur... -
+Open data
-Basic information
Entry | Database: PDB / ID: 8jyx | ||||||
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Title | Crystal structure of the gasdermin-like protein RCD-1-1 from Neurospora crassa | ||||||
Components | Maltodextrin-binding protein,Gasdermin-like protein rcd-1-1 | ||||||
Keywords | IMMUNE SYSTEM / Pyroptosis / Gasdermnin / Allorecognition | ||||||
Function / homology | Function and homology information wide pore channel activity / programmed cell death / carbohydrate transmembrane transporter activity / outer membrane-bounded periplasmic space / protein heterodimerization activity / plasma membrane / cytoplasm Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) Neurospora crassa (fungus) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.35 Å | ||||||
Authors | Li, Y. / Hou, Y.J. / Ding, J. | ||||||
Funding support | China, 1items
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Citation | Journal: Science / Year: 2024 Title: Cleavage-independent activation of ancient eukaryotic gasdermins and structural mechanisms. Authors: Yueyue Li / Yanjie Hou / Qi Sun / Huan Zeng / Fanyi Meng / Xiang Tian / Qun He / Feng Shao / Jingjin Ding / Abstract: Gasdermins (GSDMs) are pore-forming proteins that execute pyroptosis for immune defense. GSDMs are two-domain proteins activated by proteolytic removal of the inhibitory domain. In this work, we ...Gasdermins (GSDMs) are pore-forming proteins that execute pyroptosis for immune defense. GSDMs are two-domain proteins activated by proteolytic removal of the inhibitory domain. In this work, we report two types of cleavage-independent GSDM activation. First, GSDM, a pore-forming domain-only protein from the basal metazoan , is a disulfides-linked autoinhibited dimer activated by reduction of the disulfides. The cryo-electron microscopy (cryo-EM) structure illustrates the assembly mechanism for the 44-mer GSDM pore. Second, RCD-1-1 and RCD-1-2, encoded by the polymorphic () gene in filamentous fungus , are also pore-forming domain-only GSDMs. RCD-1-1 and RCD-1-2, when encountering each other, form pores and cause pyroptosis, underlying allorecognition in . The cryo-EM structure reveals a pore of 11 RCD-1-1/RCD-1-2 heterodimers and a heterodimerization-triggered pore assembly mechanism. This study shows mechanistic diversities in GSDM activation and indicates versatile functions of GSDMs. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 8jyx.cif.gz | 238.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb8jyx.ent.gz | 184.4 KB | Display | PDB format |
PDBx/mmJSON format | 8jyx.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/jy/8jyx ftp://data.pdbj.org/pub/pdb/validation_reports/jy/8jyx | HTTPS FTP |
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-Related structure data
Related structure data | 8jyvC 8jywC 8jyyC 8jyzC C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
-Assembly
Deposited unit |
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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 69615.359 Da / Num. of mol.: 2 Mutation: D108A, K109A, E198A, N199A, K265A, K388A, D389A, K174A, K175A, K176A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli), (gene. exp.) Neurospora crassa (fungus) Gene: malE, NCTC8450_00456, NCTC9775_03059, rcd-1-1, NCU05712 Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: A0A376KDN7, UniProt: Q7SBA0 #2: Polysaccharide | #3: Water | ChemComp-HOH / | Has ligand of interest | N | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.78 Å3/Da / Density % sol: 55.84 % |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, sitting drop / pH: 7.4 Details: 0.1 M Bicine pH 7.4, 11% PEG 3350, 3% (w/v) D(+)-Glucose monohydrate |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: SYNCHROTRON / Site: SSRF / Beamline: BL18U1 / Wavelength: 0.97915 Å |
Detector | Type: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: Nov 25, 2022 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97915 Å / Relative weight: 1 |
Reflection | Resolution: 2.35→79.55 Å / Num. obs: 63588 / % possible obs: 99.9 % / Redundancy: 6.8 % / Biso Wilson estimate: 45.4 Å2 / CC1/2: 0.998 / Rmerge(I) obs: 0.09 / Rpim(I) all: 0.037 / Rrim(I) all: 0.098 / Net I/σ(I): 12.3 |
Reflection shell | Resolution: 2.35→2.41 Å / Redundancy: 6.9 % / Rmerge(I) obs: 0.82 / Mean I/σ(I) obs: 2.2 / Num. unique obs: 4459 / CC1/2: 0.881 / Rpim(I) all: 0.465 / Rrim(I) all: 0.886 / % possible all: 100 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.35→45.96 Å / SU ML: 0.3492 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 30.9576 Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 58.05 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.35→45.96 Å
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Refine LS restraints |
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LS refinement shell |
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