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Open data
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Basic information
Entry | Database: PDB / ID: 1tyu | |||||||||
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Title | STRUCTURE OF TAILSPIKE-PROTEIN | |||||||||
![]() | TAILSPIKE PROTEIN | |||||||||
![]() | VIRAL ADHESION PROTEIN / COMPLEX / RECEPTOR / ENDOGLYCOSIDASE CARBOHYDRATE / CELL RECEPTOR / RECOGNITION / BINDING PROTEIN LIPOPOLYSACCHARIDE | |||||||||
Function / homology | ![]() endo-1,3-alpha-L-rhamnosidase activity / symbiont entry into host cell via disruption of host cell envelope lipopolysaccharide / virus tail, fiber / symbiont entry into host cell via disruption of host cell envelope / symbiont entry into host / Hydrolases; Glycosylases; Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds / adhesion receptor-mediated virion attachment to host cell / virion attachment to host cell Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | ![]() | |||||||||
![]() | Steinbacher, S. / Huber, R. | |||||||||
![]() | ![]() Title: Crystal structure of phage P22 tailspike protein complexed with Salmonella sp. O-antigen receptors. Authors: Steinbacher, S. / Baxa, U. / Miller, S. / Weintraub, A. / Seckler, R. / Huber, R. #1: ![]() Title: Interactions of Phage P22 Tails with Their Cellular Receptor, Salmonella O-Antigen Polysaccharide Authors: Baxa, U. / Steinbacher, S. / Miller, S. / Weintraub, A. / Huber, R. / Seckler, R. #2: ![]() Title: Crystal Structure of P22 Tailspike Protein: Interdigitated Subunits in a Thermostable Trimer Authors: Steinbacher, S. / Seckler, R. / Miller, S. / Steipe, B. / Huber, R. / Reinemer, P. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 123.3 KB | Display | ![]() |
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PDB format | ![]() | 92.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 456.8 KB | Display | ![]() |
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Full document | ![]() | 460.3 KB | Display | |
Data in XML | ![]() | 11.7 KB | Display | |
Data in CIF | ![]() | 19 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 59616.648 Da / Num. of mol.: 1 Fragment: RESIDUES 109-666 LACKING THE N-TERMINAL, HEAD-BINDING DOMAIN Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Polysaccharide | alpha-D-galactopyranose-(1-2)-[alpha-D-Tyvelopyranose-(1-3)]alpha-D-mannopyranose-(1-4)-alpha-L- ...alpha-D-galactopyranose-(1-2)-[alpha-D-Tyvelopyranose-(1-3)]alpha-D-mannopyranose-(1-4)-alpha-L-rhamnopyranose-(1-3)-alpha-D-galactopyranose-(1-2)-[alpha-D-Tyvelopyranose-(1-3)]alpha-D-mannopyranose-(1-4)-alpha-L-rhamnopyranose Source method: isolated from a genetically manipulated source |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.47 Å3/Da / Density % sol: 50.19 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 7.5 Details: COMPLEX FORMED BY SOAKING WITH 2MM OCTASACCHARIDE FROM SALMONELLA ENTERITIDIS AT PH 7.5 | ||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / pH: 10 / Method: vapor diffusion, hanging dropDetails: drop contained 0.005 ml of drop solution and 0.003 ml of precipitant | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Wavelength: 1.5418 |
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Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Aug 1, 1995 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Num. obs: 51290 / % possible obs: 93.5 % / Redundancy: 5.4 % / Rmerge(I) obs: 0.061 |
Reflection | *PLUS Highest resolution: 1.8 Å / Lowest resolution: 9999 Å / Num. measured all: 276996 |
Reflection shell | *PLUS Highest resolution: 1.8 Å / Lowest resolution: 18.5 Å / % possible obs: 36.5 % / Rmerge(I) obs: 0.293 |
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Processing
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Refinement | Resolution: 1.8→8 Å / σ(F): 0 /
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Refinement step | Cycle: LAST / Resolution: 1.8→8 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |