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Open data
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Basic information
Entry | Database: PDB / ID: 2f49 | ||||||
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Title | Crystal structure of Fus3 in complex with a Ste5 peptide | ||||||
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![]() | TRANSFERASE / protein-petide complex | ||||||
Function / homology | ![]() MAPK3 (ERK1) activation / phospho-PLA2 pathway / RAF-independent MAPK1/3 activation / MAPK1 (ERK2) activation / Frs2-mediated activation / ERK/MAPK targets / Signalling to ERK5 / ERKs are inactivated / Senescence-Associated Secretory Phenotype (SASP) / NCAM signaling for neurite out-growth ...MAPK3 (ERK1) activation / phospho-PLA2 pathway / RAF-independent MAPK1/3 activation / MAPK1 (ERK2) activation / Frs2-mediated activation / ERK/MAPK targets / Signalling to ERK5 / ERKs are inactivated / Senescence-Associated Secretory Phenotype (SASP) / NCAM signaling for neurite out-growth / Recycling pathway of L1 / Signal transduction by L1 / RAF/MAP kinase cascade / MAP2K and MAPK activation / Negative feedback regulation of MAPK pathway / Negative regulation of MAPK pathway / Gastrin-CREB signalling pathway via PKC and MAPK / Estrogen-stimulated signaling through PRKCZ / Ca2+ pathway / pheromone response MAPK cascade / pheromone-dependent signal transduction involved in conjugation with cellular fusion / invasive growth in response to glucose limitation / Regulation of HSF1-mediated heat shock response / Activation of the AP-1 family of transcription factors / retrotransposon silencing / mating projection tip / negative regulation of MAPK cascade / MAPK6/MAPK4 signaling / MAP kinase activity / mitogen-activated protein kinase / Neutrophil degranulation / positive regulation of protein export from nucleus / cytoplasmic stress granule / periplasmic space / protein kinase activity / intracellular signal transduction / cell cycle / phosphorylation / cell division / protein serine kinase activity / protein serine/threonine kinase activity / mitochondrion / ATP binding / identical protein binding / nucleus / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Remenyi, A. | ||||||
![]() | ![]() Title: The Ste5 scaffold allosterically modulates signaling output of the yeast mating pathway Authors: Bhattacharyya, R.P. / Remenyi, A. / Good, M.C. / Bashor, C.J. / Falick, A.M. / Lim, W.A. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 161.2 KB | Display | ![]() |
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PDB format | ![]() | 125.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 459.5 KB | Display | ![]() |
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Full document | ![]() | 472.8 KB | Display | |
Data in XML | ![]() | 32.3 KB | Display | |
Data in CIF | ![]() | 47 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2f9gC ![]() 2fa2C ![]() 2b9fS S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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2 | ![]()
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3 |
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4 | ![]()
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5 | ![]()
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Unit cell |
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Details | The biological unit is a protein-peptide complex between chain A and C |
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Components
#1: Protein | Mass: 40809.047 Da / Num. of mol.: 2 / Fragment: Fus3 / Mutation: T180V, Y182F Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: FUS3, DAC2 / Plasmid: pBH4-Fus3 / Production host: ![]() ![]() #2: Protein/peptide | | Mass: 3349.769 Da / Num. of mol.: 1 / Fragment: Fus3 binding region of STE5 / Source method: obtained synthetically Details: This peptide was chemically synthesized but this sequence naturally occurs in the Ste5 protein from S. cerevisiae #3: Chemical | #4: Chemical | ChemComp-SCN / #5: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.69 Å3/Da / Density % sol: 54.33 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion / pH: 6.1 Details: 18% PEG3350, 0.1M Mes, 10% MPD, 0.2M KSCN, pH 6.1, VAPOR DIFFUSION, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Mar 13, 2004 |
Radiation | Monochromator: double crystal / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.1159 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→50 Å / Num. all: 69388 / Num. obs: 69388 / % possible obs: 95.3 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 4.4 % / Rsym value: 0.07 / Net I/σ(I): 15.3 |
Reflection shell | Resolution: 1.9→1.97 Å / Mean I/σ(I) obs: 2.4 / Num. unique all: 5920 / Rsym value: 0.5 / % possible all: 83.2 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB entry 2B9F Resolution: 1.9→20 Å / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 1.9→20 Å
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Refine LS restraints |
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