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Academic Journal

Peri active site catalysis of proline isomerisation is the molecular basis of allomorphy in β-phosphoglucomutase.

  • Authors : Cruz-Navarrete FA; School of Biosciences, University of Sheffield, Sheffield, S10 2TN, UK.; Department of Structural Biology, St. Jude Children's Research Hospital, Memphis, TN, 38105, USA.

Subjects: Phosphoglucomutase*/Phosphoglucomutase*/Phosphoglucomutase*/metabolism ; Phosphoglucomutase*/Phosphoglucomutase*/Phosphoglucomutase*/chemistry ; Phosphoglucomutase*/Phosphoglucomutase*/Phosphoglucomutase*/genetics

  • Source: Communications biology [Commun Biol] 2024 Jul 27; Vol. 7 (1), pp. 909. Date of Electronic Publication: 2024 Jul 27.Publisher: Nature Publishing Group UK Country of Publication: England NLM ID: 101719179 Publication Model: Electronic Cited Medium: Internet ISSN:

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Academic Journal

The crystal structure of GH57 family amylopullulanase reveals its dual binding pockets sharing the same catalytic dyad.

  • Authors : Zhu Z; Shanghai Institute of Applied Physics, Chinese Academy of Sciences, Shanghai, China.; University of Chinese Academy of Sciences, Beijing, China.

Subjects: Glycoside Hydrolases*/Glycoside Hydrolases*/Glycoside Hydrolases*/chemistry ; Glycoside Hydrolases*/Glycoside Hydrolases*/Glycoside Hydrolases*/metabolism ; Glycoside Hydrolases*/Glycoside Hydrolases*/Glycoside Hydrolases*/genetics

  • Source: Communications biology [Commun Biol] 2025 May 26; Vol. 8 (1), pp. 806. Date of Electronic Publication: 2025 May 26.Publisher: Nature Publishing Group UK Country of Publication: England NLM ID: 101719179 Publication Model: Electronic Cited Medium: Internet ISSN:

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Academic Journal

Crystal structures of monomeric BsmI restriction endonuclease reveal coordinated sequential cleavage of two DNA strands.

  • Authors : Sieskind R; Institut Pasteur, Université Paris Cité, CNRS UMR 3528, Unit of Architecture and Dynamics of Biological Macromolecules, 75724, Paris, France.; Missoury S

Subjects: Deoxyribonucleases, Type II Site-Specific*/Deoxyribonucleases, Type II Site-Specific*/Deoxyribonucleases, Type II Site-Specific*/chemistry ; Deoxyribonucleases, Type II Site-Specific*/Deoxyribonucleases, Type II Site-Specific*/Deoxyribonucleases, Type II Site-Specific*/metabolism ; Deoxyribonucleases, Type II Site-Specific*/Deoxyribonucleases, Type II Site-Specific*/Deoxyribonucleases, Type II Site-Specific*/genetics

  • Source: Communications biology [Commun Biol] 2025 Mar 07; Vol. 8 (1), pp. 387. Date of Electronic Publication: 2025 Mar 07.Publisher: Nature Publishing Group UK Country of Publication: England NLM ID: 101719179 Publication Model: Electronic Cited Medium: Internet ISSN:

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Academic Journal

Characterization of a second class Ie ribonucleotide reductase.

  • Authors : John J; Department of Biochemistry and Biophysics, Stockholm University, Arrhenius Laboratories for Natural Sciences, Stockholm, Sweden.; Lundin D

Subjects: Ribonucleotide Reductases*/Ribonucleotide Reductases*/Ribonucleotide Reductases*/metabolism ; Ribonucleotide Reductases*/Ribonucleotide Reductases*/Ribonucleotide Reductases*/genetics ; Ribonucleotide Reductases*/Ribonucleotide Reductases*/Ribonucleotide Reductases*/chemistry

  • Source: Communications biology [Commun Biol] 2025 Feb 22; Vol. 8 (1), pp. 281. Date of Electronic Publication: 2025 Feb 22.Publisher: Nature Publishing Group UK Country of Publication: England NLM ID: 101719179 Publication Model: Electronic Cited Medium: Internet ISSN:

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Academic Journal

Structural studies reveal flexible roof of active site responsible for ω-transaminase CrmG overcoming by-product inhibition.

  • Authors : Xu J; State Key Laboratory of Respiratory Disease, Guangzhou Institutes of Biomedicine and Health, Chinese Academy of Sciences, 510530, Guangzhou, China. .; Tang X

Subjects: Catalytic Domain*; Bacterial Proteins/Bacterial Proteins/Bacterial Proteins/*chemistry ; Enzyme Inhibitors/Enzyme Inhibitors/Enzyme Inhibitors/*chemistry Actinoalloteichus cyanogriseus

  • Source: Communications biology [Commun Biol] 2020 Aug 19; Vol. 3 (1), pp. 455. Date of Electronic Publication: 2020 Aug 19.Publisher: Nature Publishing Group UK Country of Publication: England NLM ID: 101719179 Publication Model: Electronic Cited Medium: Internet ISSN:

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Academic Journal

Structural insights into the enzymatic breakdown of azomycin-derived antibiotics by 2-nitroimdazole hydrolase (NnhA).

  • Authors : Ahmed FH; Environment, CSIRO, Canberra, ACT, 2601, Australia. .; Advanced Engineering Biology Future Science Platform, CSIRO, Canberra, ACT, 2601, Australia. .

Subjects: Hydrolases*/Hydrolases*/Hydrolases*/metabolism ; Hydrolases*/Hydrolases*/Hydrolases*/chemistry ; Anti-Bacterial Agents*/Anti-Bacterial Agents*/Anti-Bacterial Agents*/metabolism

  • Source: Communications biology [Commun Biol] 2024 Dec 19; Vol. 7 (1), pp. 1676. Date of Electronic Publication: 2024 Dec 19.Publisher: Nature Publishing Group UK Country of Publication: England NLM ID: 101719179 Publication Model: Electronic Cited Medium: Internet ISSN:

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Academic Journal

Allostery in homodimeric SARS-CoV-2 main protease.

  • Authors : Fornasier E; Department of Chemical Sciences, University of Padova, via F. Marzolo 1, 35131, Padova, Italy.; Fabbian S

Subjects: SARS-CoV-2*/SARS-CoV-2*/SARS-CoV-2*/enzymology ; Coronavirus 3C Proteases*/Coronavirus 3C Proteases*/Coronavirus 3C Proteases*/metabolism ; Coronavirus 3C Proteases*/Coronavirus 3C Proteases*/Coronavirus 3C Proteases*/chemistry

  • Source: Communications biology [Commun Biol] 2024 Nov 04; Vol. 7 (1), pp. 1435. Date of Electronic Publication: 2024 Nov 04.Publisher: Nature Publishing Group UK Country of Publication: England NLM ID: 101719179 Publication Model: Electronic Cited Medium: Internet ISSN:

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Academic Journal

Structures of β-glycosidase LXYL-P1-2 reveals the product binding state of GH3 family and a specific pocket for Taxol recognition.

  • Authors : Yang L; National Research Laboratory for Physical Sciences in Microscales, University of Science and Technology of China, 230026, Hefei, Anhui, China.; Chen TJ

Subjects: Catalytic Domain* ; Models, Molecular* ; Molecular Conformation*

  • Source: Communications biology [Commun Biol] 2020 Jan 10; Vol. 3 (1), pp. 22. Date of Electronic Publication: 2020 Jan 10.Publisher: Nature Publishing Group UK Country of Publication: England NLM ID: 101719179 Publication Model: Electronic Cited Medium: Internet ISSN:

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Academic Journal

Collective exchange processes reveal an active site proton cage in bacteriorhodopsin.

  • Authors : Friedrich D; Leibniz-Forschungsinstitut für Molekulare Pharmakologie, Robert-Rössle-Str. 10, 13125, Berlin, Germany.; Freie Universität Berlin, Institut für Chemie und Biochemie, 14195, Berlin, Germany.

Subjects: Catalytic Domain* ; Models, Molecular* ; Protein Conformation*

  • Source: Communications biology [Commun Biol] 2020 Jan 03; Vol. 3 (1), pp. 4. Date of Electronic Publication: 2020 Jan 03.Publisher: Nature Publishing Group UK Country of Publication: England NLM ID: 101719179 Publication Model: Electronic Cited Medium: Internet ISSN:

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