[English] 日本語
Yorodumi- PDB-5ii4: Crystal structure of red abalone VERL repeat 1 with linker at 2.0... -
+Open data
-Basic information
Entry | Database: PDB / ID: 5ii4 | |||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Title | Crystal structure of red abalone VERL repeat 1 with linker at 2.0 A resolution | |||||||||||||||||||||
Components | Maltose-binding periplasmic protein,Vitelline envelope sperm lysin receptor | |||||||||||||||||||||
Keywords | CELL ADHESION / FERTILIZATION / EGG-SPERM INTERACTION / GAMETE RECOGNITION / VITELLINE ENVELOPE / SPERM RECEPTOR | |||||||||||||||||||||
Function / homology | Function and homology information vitelline envelope / sperm-egg recognition / carbohydrate transmembrane transporter activity / outer membrane-bounded periplasmic space / extracellular region / plasma membrane Similarity search - Function | |||||||||||||||||||||
Biological species | Escherichia coli O157:H7 (bacteria) Haliotis rufescens (red abalone) Escherichia coli (E. coli) | |||||||||||||||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2 Å | |||||||||||||||||||||
Authors | Sadat Al-Hosseini, H. / Raj, I. / Nishimura, K. / Jovine, L. | |||||||||||||||||||||
Funding support | Sweden, 6items
| |||||||||||||||||||||
Citation | Journal: Cell / Year: 2017 Title: Structural Basis of Egg Coat-Sperm Recognition at Fertilization. Authors: Raj, I. / Sadat Al Hosseini, H. / Dioguardi, E. / Nishimura, K. / Han, L. / Villa, A. / de Sanctis, D. / Jovine, L. #1: Journal: Mol. Biol. Evol. / Year: 2011 Title: The molecular basis of sex: linking yeast to human. Authors: Swanson, W.J. / Aagaard, J.E. / Vacquier, V.D. / Monne, M. / Sadat Al Hosseini, H. / Jovine, L. #2: Journal: Proc. Natl. Acad. Sci. U.S.A. / Year: 2006 Title: Rapidly evolving zona pellucida domain proteins are a major component of the vitelline envelope of abalone eggs. Authors: Aagaard, J.E. / Yi, X. / MacCoss, M.J. / Swanson, W.J. #3: Journal: Gene / Year: 2002 Title: Full-length sequence of VERL, the egg vitelline envelope receptor for abalone sperm lysin. Authors: Galindo, B.E. / Moy, G.W. / Swanson, W.J. / Vacquier, V.D. #4: Journal: Proc. Natl. Acad. Sci. U.S.A. / Year: 1997 Title: The abalone egg vitelline envelope receptor for sperm lysin is a giant multivalent molecule. Authors: Swanson, W.J. / Vacquier, V.D. | |||||||||||||||||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 5ii4.cif.gz | 286.8 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb5ii4.ent.gz | 235.6 KB | Display | PDB format |
PDBx/mmJSON format | 5ii4.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ii/5ii4 ftp://data.pdbj.org/pub/pdb/validation_reports/ii/5ii4 | HTTPS FTP |
---|
-Related structure data
Related structure data | 5ii5C 5ii6C 5ii7C 5ii8C 5ii9C 5iiaC 5iibC 5iicC 5mr2C 5mr3C 3setS 3sexS 4wrnS C: citing same article (ref.) S: Starting model for refinement |
---|---|
Similar structure data |
-Links
-Assembly
Deposited unit |
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
|
-Components
#1: Protein | Mass: 56604.797 Da / Num. of mol.: 1 Mutation: N4115Q, N4122T, N4142Y, N4171Q,N4115Q, N4122T, N4142Y, N4171Q,N4115Q, N4122T, N4142Y, N4171Q,N4115Q, N4122T, N4142Y, N4171Q Source method: isolated from a genetically manipulated source Details: THIS PROTEIN IS A CHIMERA. RESIDUES 3668-4034 ARE FROM E. COLI MALTOSE BINDING PROTEIN (MBP), CORRESPOND TO RESIDUES 27-393 OF SWISS-PROT DATABASE ENTRY P0AEX9 AND CONTAIN MUTATIONS I3669T, ...Details: THIS PROTEIN IS A CHIMERA. RESIDUES 3668-4034 ARE FROM E. COLI MALTOSE BINDING PROTEIN (MBP), CORRESPOND TO RESIDUES 27-393 OF SWISS-PROT DATABASE ENTRY P0AEX9 AND CONTAIN MUTATIONS I3669T, D3749A, K3750A, E3839A, N3840A, A3882H, K3886H, K3906A, A3979V, I3984V, E4026A, E4029A, D4030A AND R4034N (CORRESPONDING TO I28T, D108A, K109A, E198A, N199A, A241H, K245H, K265A, A338V, I343V, E385A, E388A, D389A AND R393N IN P0AEX9). RESIDUES 4038-4175 ARE FROM RED ABALONE VITELLINE ENVELOPE SPERM LYSIN RECEPTOR AND CORRESPOND TO RESIDUES 38-175 OF SWISS-PROT DATABASE ENTRY Q8WR62 AND CONTAIN MUTATIONS N4115Q, N4122T, N4142Y AND N4171Q (CORRESPONDING TO N115Q, N122T, N142Y AND N171Q). Source: (gene. exp.) Escherichia coli O157:H7 (bacteria), (gene. exp.) Haliotis rufescens (red abalone) Gene: malE, Z5632, ECs5017, VERL / Plasmid: pHLsec / Cell line (production host): HEK-293T / Production host: Homo sapiens (human) / References: UniProt: P0AEY0, UniProt: Q8WR62 | ||
---|---|---|---|
#2: Polysaccharide | alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose / alpha-maltose | ||
#3: Chemical | ChemComp-PGE / Mass: 150.173 Da / Num. of mol.: 5 / Mutation: N4115Q, N4122T, N4142Y, N4171Q Source method: isolated from a genetically manipulated source Formula: C6H14O4 Details: THIS PROTEIN IS A CHIMERA. RESIDUES 3668-4034 ARE FROM E. COLI MALTOSE BINDING PROTEIN (MBP), CORRESPOND TO RESIDUES 27-393 OF SWISS-PROT DATABASE ENTRY P0AEX9 AND CONTAIN MUTATIONS I3669T, ...Details: THIS PROTEIN IS A CHIMERA. RESIDUES 3668-4034 ARE FROM E. COLI MALTOSE BINDING PROTEIN (MBP), CORRESPOND TO RESIDUES 27-393 OF SWISS-PROT DATABASE ENTRY P0AEX9 AND CONTAIN MUTATIONS I3669T, D3749A, K3750A, E3839A, N3840A, A3882H, K3886H, K3906A, A3979V, I3984V, E4026A, E4029A, D4030A AND R4034N (CORRESPONDING TO I28T, D108A, K109A, E198A, N199A, A241H, K245H, K265A, A338V, I343V, E385A, E388A, D389A AND R393N IN P0AEX9). RESIDUES 4038-4175 ARE FROM RED ABALONE VITELLINE ENVELOPE SPERM LYSIN RECEPTOR AND CORRESPOND TO RESIDUES 38-175 OF SWISS-PROT DATABASE ENTRY Q8WR62 AND CONTAIN MUTATIONS N4115Q, N4122T, N4142Y AND N4171Q (CORRESPONDING TO N115Q, N122T, N142Y AND N171Q). Source: (gene. exp.) Escherichia coli (E. coli) / Gene: malE / Plasmid: pHLsec / Cell line (production host): HEK-293T / Production host: Homo sapiens (human) #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
---|
-Sample preparation
Crystal | Density Matthews: 2.87 Å3/Da / Density % sol: 57.2 % |
---|---|
Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 9.5 / Details: 40% PEG 600, 0.1M CHES |
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID29 / Wavelength: 0.97625 Å |
Detector | Type: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: Sep 10, 2014 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97625 Å / Relative weight: 1 |
Reflection | Resolution: 2→46.991 Å / Num. obs: 44601 / % possible obs: 98 % / Redundancy: 4.9 % / Biso Wilson estimate: 36.16 Å2 / Rmerge(I) obs: 0.1027 / Net I/σ(I): 8.84 |
Reflection shell | Resolution: 2→2.072 Å / Redundancy: 4.7 % / Rmerge(I) obs: 1.446 / Mean I/σ(I) obs: 1.01 / % possible all: 98 |
-Processing
Software |
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 3SET, 3SEX and 4WRN Resolution: 2→46.991 Å / SU ML: 0.28 / Cross valid method: FREE R-VALUE / σ(F): 1.39 / Phase error: 27.97
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | Shrinkage radii: 0.7 Å / VDW probe radii: 1.1 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2→46.991 Å
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell |
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement TLS group |
|