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- PDB-1l17: HYDROPHOBIC STABILIZATION IN T4 LYSOZYME DETERMINED DIRECTLY BY M... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1l17 | |||||||||
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Title | HYDROPHOBIC STABILIZATION IN T4 LYSOZYME DETERMINED DIRECTLY BY MULTIPLE SUBSTITUTIONS OF ILE 3 | |||||||||
![]() | T4 LYSOZYME | |||||||||
![]() | HYDROLASE (O-GLYCOSYL) | |||||||||
Function / homology | ![]() viral release from host cell by cytolysis / peptidoglycan catabolic process / cell wall macromolecule catabolic process / lysozyme / lysozyme activity / host cell cytoplasm / defense response to bacterium Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | ![]() | |||||||||
![]() | Matsumura, M. / Dao-Pin, S. / Matthews, B.W. | |||||||||
![]() | ![]() Title: Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3. Authors: Matsumura, M. / Becktel, W.J. / Matthews, B.W. #1: ![]() Title: Structural Studies of Mutants of T4 Lysozyme that Alter Hydrophobic Stabilization Authors: Matsumura, M. / Wozniak, J.A. / Dao-Pin, S. / Matthews, B.W. #2: ![]() Title: High-Resolution Structure of the Temperature-Sensitive Mutant of Phage Lysozyme, Arg 96 (Right Arrow) His Authors: Weaver, L.H. / Gray, T.M. / Gruetter, M.G. / Anderson, D.E. / Wozniak, J.A. / Dahlquist, F.W. / Matthews, B.W. #3: ![]() Title: Contributions of Left-Handed Helical Residues to the Structure and Stability of Bacteriophage T4 Lysozyme Authors: Nicholson, H. / Soderlind, E. / Tronrud, D.E. / Matthews, B.W. #4: ![]() Title: Enhanced Protein Thermostability from Designed Mutations that Interact with Alpha-Helix Dipoles Authors: Nicholson, H. / Becktel, W.J. / Matthews, B.W. #5: ![]() Title: Replacements of Pro86 in Phage T4 Lysozyme Extend an Alpha-Helix But Do not Alter Protein Stability Authors: Alber, T. / Bell, J.A. / Dao-Pin, S. / Nicholson, H. / Wozniak, J.A. / Cook, S. / Matthews, B.W. #6: ![]() Title: Enhanced Protein Thermostability from Site-Directed Mutations that Decrease the Entropy of Unfolding Authors: Matthews, B.W. / Nicholson, H. / Becktel, W.J. #7: ![]() Title: Structural Analysis of the Temperature-Sensitive Mutant of Bacteriophage T4 Lysozyme, Glycine 156 (Right Arrow) Aspartic Acid Authors: Gray, T.M. / Matthews, B.W. #8: ![]() Title: Contributions of Hydrogen Bonds of Thr 157 to the Thermodynamic Stability of Phage T4 Lysozyme Authors: Alber, T. / Dao-Pin, S. / Wilson, K. / Wozniak, J.A. / Cook, S.P. / Matthews, B.W. #9: ![]() Title: Structural Studies of Mutants of the Lysozyme of Bacteriophage T4. The Temperature-Sensitive Mutant Protein Thr157 (Right Arrow) Ile Authors: Gruetter, M.G. / Gray, T.M. / Weaver, L.H. / Alber, T. / Wilson, K. / Matthews, B.W. #10: ![]() Title: Structure of Bacteriophage T4 Lysozyme Refined at 1.7 Angstroms Resolution Authors: Weaver, L.H. / Matthews, B.W. #11: ![]() Title: Temperature-Sensitive Mutations of Bacteriophage T4 Lysozyme Occur at Sites with Low Mobility and Low Solvent Accessibility in the Folded Protein Authors: Alber, T. / Dao-Pin, S. / Nye, J.A. / Muchmore, D.C. / Matthews, B.W. #12: ![]() Title: Common Precursor of Lysozymes of Hen Egg-White and Bacteriophage T4 Authors: Matthews, B.W. / Gruetter, M.G. / Anderson, W.F. / Remington, S.J. #13: ![]() Title: Crystallographic Determination of the Mode of Binding of Oligosaccharides to T4 Bacteriophage Lysozyme. Implications for the Mechanism of Catalysis Authors: Anderson, W.F. / Gruetter, M.G. / Remington, S.J. / Weaver, L.H. / Matthews, B.W. #14: ![]() Title: Relation between Hen Egg White Lysozyme and Bacteriophage T4 Lysozyme. Evolutionary Implications Authors: Matthews, B.W. / Remington, S.J. / Gruetter, M.G. / Anderson, W.F. #15: ![]() Title: Structure of the Lysozyme from Bacteriophage T4, an Electron Density Map at 2.4 Angstroms Resolution Authors: Remington, S.J. / Anderson, W.F. / Owen, J. / Teneyck, L.F. / Grainger, C.T. / Matthews, B.W. #16: ![]() Title: Atomic Coordinates for T4 Phage Lysozyme Authors: Remington, S.J. / Teneyck, L.F. / Matthews, B.W. #17: ![]() Title: Comparison of the Predicted and Observed Secondary Structure of T4 Phage Lysozyme Authors: Matthews, B.W. #18: ![]() Title: The Three Dimensional Structure of the Lysozyme from Bacteriophage T4 Authors: Matthews, B.W. / Remington, S.J. #19: ![]() Title: Crystallographic Data for Lysozyme from Bacteriophage T4 Authors: Matthews, B.W. / Dahlquist, F.W. / Maynard, A.Y. | |||||||||
History |
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Remark 700 | SHEET THERE ARE SEVERAL SUBTLE ASPECTS OF THE SECONDARY STRUCTURE OF THIS MOLECULE WHICH CANNOT ...SHEET THERE ARE SEVERAL SUBTLE ASPECTS OF THE SECONDARY STRUCTURE OF THIS MOLECULE WHICH CANNOT CONVENIENTLY BE REPRESENTED IN THE HELIX AND SHEET RECORDS BELOW. THESE ASPECTS INFLUENCE THE REPRESENTATION OF HELIX 6 AND STRAND 3 OF SHEET *S1*. THE PAPER CITED IN REFERENCE 15 ABOVE SHOULD BE CONSULTED FOR THESE SUBTLETIES. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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PDBx/mmCIF format | ![]() | 49.2 KB | Display | ![]() |
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PDB format | ![]() | 35.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-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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Atom site foot note | 1: SEE REMARK 6. |
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Components
#1: Protein | Mass: 18648.439 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.79 Å3/Da / Density % sol: 55.88 % | ||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 6.7 / Method: batch methodDetails: taken from Remington, S.J. et al (1978). J. Mol. Biol., 81-98. | ||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 1.7 Å |
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Processing
Software | Name: TNT / Classification: refinement | ||||||||||||
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Refinement | Resolution: 1.7→6 Å / Rfactor obs: 0.157 Details: RESIDUES 162 - 164 IN WILD-TYPE AND ALL MUTANT LYSOZYMES ARE EXTREMELY MOBILE. THUS THE COORDINATES FOR THESE RESIDUES ARE VERY UNRELIABLE. | ||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.7→6 Å
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