+Open data
-Basic information
Entry | Database: PDB / ID: 3v2y | ||||||
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Title | Crystal Structure of a Lipid G protein-Coupled Receptor at 2.80A | ||||||
Components | Sphingosine 1-phosphate receptor 1, Lysozyme chimera (E.C.3.2.1.17) | ||||||
Keywords | HYDROLASE / sphingosine / EDG receptor / lipid receptor / multiple sclerosis / autoimmunity / Structural Genomics / PSI-Biology / GPCR Network / GPCR / membrane protein / G protein coupled receptor / membrane | ||||||
Function / homology | Function and homology information cardiac muscle tissue growth involved in heart morphogenesis / sphingosine-1-phosphate receptor activity / sphingolipid binding / blood vessel maturation / Lysosphingolipid and LPA receptors / T cell migration / endothelial cell differentiation / heart trabecula morphogenesis / regulation of metabolic process / regulation of bone mineralization ...cardiac muscle tissue growth involved in heart morphogenesis / sphingosine-1-phosphate receptor activity / sphingolipid binding / blood vessel maturation / Lysosphingolipid and LPA receptors / T cell migration / endothelial cell differentiation / heart trabecula morphogenesis / regulation of metabolic process / regulation of bone mineralization / sphingosine-1-phosphate receptor signaling pathway / leukocyte chemotaxis / regulation of bone resorption / positive regulation of positive chemotaxis / lamellipodium assembly / negative regulation of stress fiber assembly / transmission of nerve impulse / regulation of cell adhesion / viral release from host cell by cytolysis / adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway / peptidoglycan catabolic process / G protein-coupled receptor binding / G protein-coupled receptor activity / positive regulation of smooth muscle cell proliferation / brain development / adenylate cyclase-activating G protein-coupled receptor signaling pathway / neuron differentiation / chemotaxis / cell migration / cell wall macromolecule catabolic process / lysozyme / lysozyme activity / phospholipase C-activating G protein-coupled receptor signaling pathway / actin cytoskeleton organization / angiogenesis / Interleukin-4 and Interleukin-13 signaling / cell population proliferation / host cell cytoplasm / Potential therapeutics for SARS / cell adhesion / endosome / positive regulation of cell migration / defense response to bacterium / membrane raft / G protein-coupled receptor signaling pathway / external side of plasma membrane / intracellular membrane-bounded organelle / positive regulation of transcription by RNA polymerase II / nucleoplasm / plasma membrane / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) Enterobacteria phage T4 (virus) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.8 Å | ||||||
Authors | Hanson, M.A. / Roth, C.B. / Jo, E. / Griffith, M.T. / Scott, F.L. / Reinhart, G. / Desale, H. / Clemons, B. / Cahalan, S.M. / Schuerer, S.C. ...Hanson, M.A. / Roth, C.B. / Jo, E. / Griffith, M.T. / Scott, F.L. / Reinhart, G. / Desale, H. / Clemons, B. / Cahalan, S.M. / Schuerer, S.C. / Sanna, M.G. / Han, G.W. / Kuhn, P. / Rosen, H. / Stevens, R.C. / GPCR Network (GPCR) | ||||||
Citation | Journal: Science / Year: 2012 Title: Crystal structure of a lipid G protein-coupled receptor. Authors: Hanson, M.A. / Roth, C.B. / Jo, E. / Griffith, M.T. / Scott, F.L. / Reinhart, G. / Desale, H. / Clemons, B. / Cahalan, S.M. / Schuerer, S.C. / Sanna, M.G. / Han, G.W. / Kuhn, P. / Rosen, H. / Stevens, R.C. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3v2y.cif.gz | 193.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3v2y.ent.gz | 152.6 KB | Display | PDB format |
PDBx/mmJSON format | 3v2y.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/v2/3v2y ftp://data.pdbj.org/pub/pdb/validation_reports/v2/3v2y | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Components on special symmetry positions |
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Details | THE AUTHOR STATES THAT THE BIOLOGICAL UNIT OF THIS PROTEIN IS UNKNOWN. |
-Components
#1: Protein | Mass: 58973.168 Da / Num. of mol.: 1 / Mutation: C1054T, C1097A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human), (gene. exp.) Enterobacteria phage T4 (virus) Gene: S1PR1, CHEDG1, EDG1 / Plasmid: pFASTBAC / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: P21453, UniProt: P00720, lysozyme |
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#2: Chemical | ChemComp-ML5 / {( |
#3: Sugar | ChemComp-NAG / |
#4: Water | ChemComp-HOH / |
Sequence details | THE AUTHORS STATE THAT THE SEQUENCE "NV" IS THE ORIGINAL SEQUENCE FROM ENDOTHELIUM, AS OPPOSED TO ...THE AUTHORS STATE THAT THE SEQUENCE "NV" IS THE ORIGINAL SEQUENCE FROM ENDOTHELIU |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 77 |
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-Sample preparation
Crystal | Density Matthews: 2.61 Å3/Da / Density % sol: 52.93 % |
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Crystal grow | Temperature: 287 K / Method: lipidic cubic phase Details: 0.1M Tricine, 34-36% PEG400, 80mM sodium citrate and 4% glycerol, Lipid cubic phase, temperature 287K |
-Data collection
Diffraction |
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Diffraction source |
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Detector | Type: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Jan 1, 2009 | ||||||||||||
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | ||||||||||||
Radiation wavelength | Relative weight: 1 | ||||||||||||
Reflection | Resolution: 2.8→20 Å / Num. obs: 15297 / % possible obs: 97.2 % / Redundancy: 6 % / Biso Wilson estimate: 34.3 Å2 / Rmerge(I) obs: 0.16 / Net I/σ(I): 6.1 | ||||||||||||
Reflection shell | Resolution: 2.8→2.95 Å / Redundancy: 3.1 % / Rmerge(I) obs: 0.42 / Mean I/σ(I) obs: 1.9 / % possible all: 94.4 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 7TM of b2AR and T4L Resolution: 2.8→19.52 Å / Cor.coef. Fo:Fc: 0.9055 / Cor.coef. Fo:Fc free: 0.8586 / Cross valid method: THROUGHOUT / σ(F): 0
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Displacement parameters | Biso mean: 76.61 Å2
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Refine analyze | Luzzati coordinate error obs: 0.44 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.8→19.52 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.8→2.99 Å / Total num. of bins used: 8
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Refinement TLS params. | Method: refined / Origin x: 17.1445 Å / Origin y: 18.5316 Å / Origin z: 13.5414 Å
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Refinement TLS group | Selection details: chain A |