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Yorodumi- PDB-2w81: Structure of a complex between Neisseria meningitidis factor H bi... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2w81 | ||||||
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Title | Structure of a complex between Neisseria meningitidis factor H binding protein and CCPs 6-7 of human complement factor H | ||||||
Components |
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Keywords | IMMUNE SYSTEM / GLYCOPROTEIN / IMMUNE EVASION / AGE-RELATED MACULAR DEGENERATION / INNATE IMMUNITY / IMMUNE RESPONSE / DISEASE MUTATION / FACTOR H / COMPLEMENT ALTERNATE PATHWAY / VACCINE CANDIDATE | ||||||
Function / homology | Function and homology information regulation of complement activation, alternative pathway / bacterial extracellular vesicle / symbiont cell surface / complement component C3b binding / regulation of complement-dependent cytotoxicity / regulation of complement activation / heparan sulfate proteoglycan binding / serine-type endopeptidase complex / complement activation, alternative pathway / complement activation ...regulation of complement activation, alternative pathway / bacterial extracellular vesicle / symbiont cell surface / complement component C3b binding / regulation of complement-dependent cytotoxicity / regulation of complement activation / heparan sulfate proteoglycan binding / serine-type endopeptidase complex / complement activation, alternative pathway / complement activation / Regulation of Complement cascade / cell outer membrane / heparin binding / blood microparticle / proteolysis / extracellular space / extracellular exosome / extracellular region / identical protein binding Similarity search - Function | ||||||
Biological species | HOMO SAPIENS (human) NEISSERIA MENINGITIDIS (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.35 Å | ||||||
Authors | Schneider, M.C. / Prosser, B.E. / Caesar, J.J.E. / Kugelberg, E. / Li, S. / Zhang, Q. / Quoraishi, S. / Lovett, J.E. / Deane, J.E. / Sim, R.B. ...Schneider, M.C. / Prosser, B.E. / Caesar, J.J.E. / Kugelberg, E. / Li, S. / Zhang, Q. / Quoraishi, S. / Lovett, J.E. / Deane, J.E. / Sim, R.B. / Roversi, P. / Johnson, S. / Tang, C.M. / Lea, S.M. | ||||||
Citation | Journal: Nature / Year: 2009 Title: Neisseria Meningitidis Recruits Factor H Using Protein Mimicry of Host Carbohydrates. Authors: Schneider, M.C. / Prosser, B.E. / Caesar, J.J.E. / Kugelberg, E. / Li, S. / Zhang, Q. / Quoraishi, S. / Lovett, J.E. / Deane, J.E. / Sim, R.B. / Roversi, P. / Johnson, S. / Tang, C.M. / Lea, S.M. | ||||||
History |
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Remark 700 | SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "CC" IN EACH CHAIN ON SHEET RECORDS BELOW ... SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "CC" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 8-STRANDED BARREL THIS IS REPRESENTED BY A 9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "DC" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 8-STRANDED BARREL THIS IS REPRESENTED BY A 9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "FC" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 7-STRANDED BARREL THIS IS REPRESENTED BY A 8-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2w81.cif.gz | 227.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2w81.ent.gz | 182.8 KB | Display | PDB format |
PDBx/mmJSON format | 2w81.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/w8/2w81 ftp://data.pdbj.org/pub/pdb/validation_reports/w8/2w81 | HTTPS FTP |
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-Related structure data
Related structure data | 2w80C 2uwnS S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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3 |
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Unit cell |
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Components on special symmetry positions |
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-Components
#1: Protein | Mass: 14222.026 Da / Num. of mol.: 3 / Fragment: CCPS 6 AND 7, RESIDUES 321-443 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Variant: HIS 402 FORM / Plasmid: PET / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P08603 #2: Protein | Mass: 26983.078 Da / Num. of mol.: 3 Fragment: FULL PROTEIN WITHOUT SIGNAL SEQUENCE, RESIDUES 71-320 Source method: isolated from a genetically manipulated source Source: (gene. exp.) NEISSERIA MENINGITIDIS (bacteria) / Plasmid: PET / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q9JXV4 #3: Water | ChemComp-HOH / | Sequence details | FRAGMENT OF THIS ENTRY -CCPS 6 AND 7 ONLY | |
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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: 2.22 Å3/Da / Density % sol: 44.21 % / Description: NONE |
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Crystal grow | pH: 9 / Details: 20% PEG 6000, 0.1M BICINE PH 9.0 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: Diamond / Beamline: I03 / Wavelength: 0.9814 |
Detector | Type: ADSC CCD / Detector: CCD / Date: Jul 12, 2008 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9814 Å / Relative weight: 1 |
Reflection | Resolution: 2.35→40 Å / Num. obs: 43159 / % possible obs: 94.3 % / Observed criterion σ(I): 1 / Redundancy: 3.6 % / Biso Wilson estimate: 46.43 Å2 / Rmerge(I) obs: 0.05 / Net I/σ(I): 20.6 |
Reflection shell | Resolution: 2.35→2.41 Å / Redundancy: 3.7 % / Rmerge(I) obs: 0.32 / Mean I/σ(I) obs: 4.5 / % possible all: 95.5 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 2UWN Resolution: 2.35→38.81 Å / Cross valid method: THROUGHOUT / σ(F): 0 Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. THERE ARE 3 COPIES OF THE COMPLEX IN THE ASYMMETRIC UNIT, BUT SUBTLE REARRANGMENTS MEAN THAT NCS WAS NOT USED IN THE FINAL REFINEMENT
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Displacement parameters | Biso mean: 42.25 Å2
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Refinement step | Cycle: LAST / Resolution: 2.35→38.81 Å
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LS refinement shell | Resolution: 2.35→2.49 Å / Total num. of bins used: 9
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