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- PDB-5ii4: Crystal structure of red abalone VERL repeat 1 with linker at 2.0... -
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Open data
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Basic information
Entry | Database: PDB / ID: 5ii4 | |||||||||||||||||||||
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Title | Crystal structure of red abalone VERL repeat 1 with linker at 2.0 A resolution | |||||||||||||||||||||
![]() | Maltose-binding periplasmic protein,Vitelline envelope sperm lysin receptor | |||||||||||||||||||||
![]() | CELL ADHESION / FERTILIZATION / EGG-SPERM INTERACTION / GAMETE RECOGNITION / VITELLINE ENVELOPE / SPERM RECEPTOR | |||||||||||||||||||||
Function / homology | ![]() vitelline envelope / sperm-egg recognition / carbohydrate transmembrane transporter activity / maltose binding / maltose transport / maltodextrin transmembrane transport / ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing / outer membrane-bounded periplasmic space / extracellular region / plasma membrane Similarity search - Function | |||||||||||||||||||||
Biological species | ![]() ![]() ![]() ![]() ![]() | |||||||||||||||||||||
Method | ![]() ![]() ![]() | |||||||||||||||||||||
![]() | Sadat Al-Hosseini, H. / Raj, I. / Nishimura, K. / Jovine, L. | |||||||||||||||||||||
Funding support | ![]()
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![]() | ![]() 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 |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 286.8 KB | Display | ![]() |
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PDB format | ![]() | 235.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 5ii5C ![]() 5ii6C ![]() 5ii7C ![]() 5ii8C ![]() 5ii9C ![]() 5iiaC ![]() 5iibC ![]() 5iicC ![]() 5mr2C ![]() 5mr3C ![]() 3setS ![]() 3sexS ![]() 4wrnS C: citing same article ( S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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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.) ![]() ![]() ![]() Gene: malE, Z5632, ECs5017, VERL / Plasmid: pHLsec / Cell line (production host): HEK-293T / Production host: ![]() | ||
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#2: Polysaccharide | alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose / alpha-maltose | ||
#3: Chemical | ChemComp-PGE / ![]() 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.) ![]() ![]() ![]() #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.87 Å3/Da / Density % sol: 57.2 % |
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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 |
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Diffraction source | Source: ![]() ![]() ![]() |
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 |
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Processing
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Refinement | Method to determine structure: ![]() 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
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Solvent computation | Shrinkage radii: 0.7 Å / VDW probe radii: 1.1 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2→46.991 Å
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Refine LS restraints |
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LS refinement shell |
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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