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データを開く
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基本情報
登録情報 | データベース: PDB / ID: 1l60 | ||||||
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タイトル | ANALYSIS OF THE INTERACTION BETWEEN CHARGED SIDE CHAINS AND THE ALPHA-HELIX DIPOLE USING DESIGNED THERMOSTABLE MUTANTS OF PHAGE T4 LYSOZYME | ||||||
![]() | T4 LYSOZYME | ||||||
![]() | HYDROLASE (O-GLYCOSYL) | ||||||
機能・相同性 | ![]() 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 類似検索 - 分子機能 | ||||||
生物種 | ![]() | ||||||
手法 | ![]() | ||||||
![]() | Nicholson, H. / Matthews, B.W. | ||||||
![]() | ![]() タイトル: Analysis of the effectiveness of proline substitutions and glycine replacements in increasing the stability of phage T4 lysozyme. 著者: Nicholson, H. / Tronrud, D.E. / Becktel, W.J. / Matthews, B.W. #1: ![]() タイトル: Analysis of the Interaction between Charged Side Chains and the Alpha-Helix Dipole Using Designed Thermostable Mutants of Phage T4 Lysozyme 著者: Nicholson, H. / Anderson, D.E. / Dao-Pin, S. / Matthews, B.W. #2: ![]() タイトル: The Structural and Thermodynamic Consequences of Burying a Charged Residue within the Hydrophobic Core of T4 Lysozyme 著者: Daopin, S. / Anderson, E. / Baase, W. / Dahlquist, F.W. / Matthews, B.W. #3: ![]() タイトル: Multiple Stabilizing Alanine Replacements within Alpha-Helix 126-134 of T4 Lysozyme Have Independent, Additive Effects on Both Structure and Stability 著者: Zhang, X.-J. / Baase, W.A. / Matthews, B.W. #4: ![]() タイトル: Tolerance of T4 Lysozyme to Proline Substitutions within the Long Interdomain Alpha-Helix Illustrates the Adaptability of Proteins to Potentially Destabilizing Lesions 著者: Sauer, U.H. / Dao-Pin, S. / Matthews, B.W. #5: ![]() タイトル: Tolerance of T4 Lysozyme to Multiple Xaa (Right Arrow) Ala Substitutions: A Polyalanine Alpha-Helix Containing Ten Consecutive Alanines 著者: Heinz, D.W. / Baase, W.A. / Matthews, B.W. #6: ![]() タイトル: Cumulative Site-Directed Charge-Change Replacements in Bacteriophage T4 Lysozyme Suggest that Long-Range Electrostatic Interactions Contribute Little to Protein Stability 著者: Dao-Pin, S. / Soderlind, E. / Baase, W.A. / Wozniak, J.A. / Sauer, U. / Matthews, B.W. #7: ![]() タイトル: Structural and Thermodynamic Analysis of the Packing of Two Alpha-Helices in Bacteriophage T4 Lysozyme 著者: Daopin, S. / Alber, T. / Baase, W.A. / Wozniak, J.A. / Matthews, B.W. #8: ![]() タイトル: Contributions of Engineered Surface Salt Bridges to the Stability of T4 Lysozyme Determined by Directed Mutagenesis 著者: Dao-Pin, S. / Sauer, U. / Nicholson, H. / Matthews, B.W. #9: ![]() タイトル: Toward a Simplification of the Protein Folding Problem: A Stabilizing Polyalanine Alpha-Helix Engineered in T4 Lysozyme 著者: Zhang, X.-J. / Baase, W.A. / Matthews, B.W. #10: ![]() タイトル: Structure of a Thermostable Disulfide-Bridge Mutant of Phage T4 Lysozyme Shows that an Engineered Crosslink in a Flexible Region Does not Increase the Rigidity of the Folded Protein 著者: Pjura, P.E. / Matsumura, M. / Wozniak, J.A. / Matthews, B.W. #11: ![]() タイトル: Structural Studies of Mutants of T4 Lysozyme that Alter Hydrophobic Stabilization 著者: Matsumura, M. / Wozniak, J.A. / Dao-Pin, S. / Matthews, B.W. #12: ![]() タイトル: High-Resolution Structure of the Temperature-Sensitive Mutant of Phage Lysozyme, Arg 96 (Right Arrow) His 著者: Weaver, L.H. / Gray, T.M. / Gruetter, M.G. / Anderson, D.E. / Wozniak, J.A. / Dahlquist, F.W. / Matthews, B.W. #13: ![]() タイトル: Contributions of Left-Handed Helical Residues to the Structure and Stability of Bacteriophage T4 Lysozyme 著者: Nicholson, H. / Soderlind, E. / Tronrud, D.E. / Matthews, B.W. #14: ![]() タイトル: Hydrophobic Stabilization in T4 Lysozyme Determined Directly by Multiple Substitutions of Ile 3 著者: Matsumura, M. / Becktel, W.J. / Matthews, B.W. #15: ![]() タイトル: Enhanced Protein Thermostability from Designed Mutations that Interact with Alpha-Helix Dipoles 著者: Nicholson, H. / Becktel, W.J. / Matthews, B.W. #16: ![]() タイトル: Replacements of Pro86 in Phage T4 Lysozyme Extend an Alpha-Helix But Do not Alter Protein Stability 著者: Alber, T. / Bell, J.A. / Dao-Pin, S. / Nicholson, H. / Cook, J.A.Wozniak S. / Matthews, B.W. #17: ![]() タイトル: Enhanced Protein Thermostability from Site-Directed Mutations that Decrease the Entropy of Unfolding 著者: Matthews, B.W. / Nicholson, H. / Becktel, W.J. #18: ![]() タイトル: Structural Analysis of the Temperature-Sensitive Mutant of Bacteriophage T4 Lysozyme, Glycine 156 (Right Arrow) Aspartic Acid 著者: Gray, T.M. / Matthews, B.W. #19: ![]() タイトル: Contributions of Hydrogen Bonds of Thr 157 to the Thermodynamic Stability of Phage T4 Lysozyme 著者: Alber, T. / Dao-Pin, S. / Wilson, K. / Wozniak, J.A. / Cook, S.P. / Matthews, B.W. #20: ![]() タイトル: Structural Studies of Mutants of the Lysozyme of Bacteriophage T4. The Temperature-Sensitive Mutant Protein Thr157 (Right Arrow) Ile 著者: Gruetter, M.G. / Gray, T.M. / Weaver, L.H. / Alber, T. / Wilson, K. / Matthews, B.W. #21: ![]() タイトル: Structure of Bacteriophage T4 Lysozyme Refined at 1.7 Angstroms Resolution 著者: Weaver, L.H. / Matthews, B.W. #22: ![]() タイトル: Temperature-Sensitive Mutations of Bacteriophage T4 Lysozyme Occur at Sites with Low Mobility and Low Solvent Accessibility in the Folded Protein 著者: Alber, T. / Dao-Pin, S. / Nye, J.A. / Muchmore, D.C. / Matthews, B.W. #23: ![]() タイトル: Common Precursor of Lysozymes of Hen Egg-White and Bacteriophage T4 著者: Matthews, B.W. / Gruetter, M.G. / Anderson, W.F. / Remington, S.J. #24: ![]() タイトル: Crystallographic Determination of the Mode of Binding of Oligosaccharides to T4 Bacteriophage Lysozyme. Implications for the Mechanism of Catalysis 著者: Anderson, W.F. / Gruetter, M.G. / Remington, S.J. / Weaver, L.H. / Matthews, B.W. #25: ![]() タイトル: Relation between Hen Egg White Lysozyme and Bacteriophage T4 Lysozyme. Evolutionary Implications 著者: Matthews, B.W. / Remington, S.J. / Gruetter, M.G. / Anderson, W.F. #26: ![]() タイトル: Structure of the Lysozyme from Bacteriophage T4, an Electron Density Map at 2.4 Angstroms Resolution 著者: Remington, S.J. / Anderson, W.F. / Owen, J. / Teneyck, L.F. / Grainger, C.T. / Matthews, B.W. #27: ![]() タイトル: Atomic Coordinates for T4 Phage Lysozyme 著者: Remington, S.J. / Teneyck, L.F. / Matthews, B.W. #28: ![]() タイトル: Comparison of the Predicted and Observed Secondary Structure of T4 Phage Lysozyme 著者: Matthews, B.W. #29: ![]() タイトル: The Three Dimensional Structure of the Lysozyme from Bacteriophage T4 著者: Matthews, B.W. / Remington, S.J. #30: ![]() タイトル: Crystallographic Data for Lysozyme from Bacteriophage T4 著者: Matthews, B.W. / Dahlquist, F.W. / Maynard, A.Y. | ||||||
履歴 |
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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 AS REFERENCE 26 ABOVE SHOULD BE CONSULTED FOR THESE SUBTLETIES. |
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構造の表示
構造ビューア | 分子: ![]() ![]() |
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ダウンロードとリンク
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ダウンロード
PDBx/mmCIF形式 | ![]() | 49.7 KB | 表示 | ![]() |
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PDB形式 | ![]() | 35.7 KB | 表示 | ![]() |
PDBx/mmJSON形式 | ![]() | ツリー表示 | ![]() | |
その他 | ![]() |
-検証レポート
アーカイブディレクトリ | ![]() ![]() | HTTPS FTP |
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-関連構造データ
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リンク
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集合体
登録構造単位 | ![]()
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単位格子 |
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Atom site foot note | 1: RESIDUES 162 - 164 IN WILD-TYPE AND ALL MUTANT LYSOZYMES ARE EXTREMELY MOBILE. THUS THE COORDINATES FOR THESE RESIDUES ARE VERY UNRELIABLE. |
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要素
#1: タンパク質 | 分子量: 18676.492 Da / 分子数: 1 / 由来タイプ: 組換発現 由来: (組換発現) ![]() 属: T4-like viruses / 生物種: Enterobacteria phage T4 sensu lato / 器官: EGG / プラスミド: M13 / 参照: UniProt: P00720, lysozyme |
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#2: 水 | ChemComp-HOH / |
-実験情報
-実験
実験 | 手法: ![]() |
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試料調製
結晶 | マシュー密度: 2.79 Å3/Da / 溶媒含有率: 55.86 % | ||||||||||||||||||||||||||||||||||||||||||||||||
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結晶化 | *PLUS pH: 6.7 / 手法: batch method詳細: taken from Remington, S.J. et al (1978). J. Mol. Biol., 81-98. | ||||||||||||||||||||||||||||||||||||||||||||||||
溶液の組成 | *PLUS
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-データ収集
放射 | 散乱光タイプ: x-ray |
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放射波長 | 相対比: 1 |
反射 | *PLUS 最高解像度: 1.65 Å / Num. obs: 16682 / Rmerge(I) obs: 0.057 |
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解析
ソフトウェア | 名称: TNT / 分類: 精密化 | ||||||||||||||||||||||||||||||
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精密化 | 解像度: 1.7→6 Å / Rfactor obs: 0.158 詳細: RESIDUES 162 - 164 IN WILD-TYPE AND ALL MUTANT LYSOZYMES ARE EXTREMELY MOBILE. THUS THE COORDINATES FOR THESE RESIDUES ARE VERY UNRELIABLE. | ||||||||||||||||||||||||||||||
精密化ステップ | サイクル: LAST / 解像度: 1.7→6 Å
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拘束条件 |
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精密化 | *PLUS 最高解像度: 1.7 Å / 最低解像度: 6 Å / Rfactor obs: 0.158 | ||||||||||||||||||||||||||||||
溶媒の処理 | *PLUS | ||||||||||||||||||||||||||||||
原子変位パラメータ | *PLUS | ||||||||||||||||||||||||||||||
拘束条件 | *PLUS
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