The structure of the Staphylococcus aureus sortase-substrate complex reveals how the universally conserved LPXTG sorting signal is recognized (Q24651383)

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The Structure of the Staphylococcus aureus Sortase-Substrate Complex Reveals How the Universally Conserved LPXTG Sorting Signal Is Recognized

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English	The structure of the Staphylococcus aureus sortase-substrate complex reveals how the universally conserved LPXTG sorting signal is recognized	scientific article	The Structure of the Staphylococcus aureus Sortase-Substrate Complex Reveals How the Universally Conserved LPXTG Sorting Signal Is Recognized

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2 February 2020

The structure of the Staphylococcus aureus sortase-substrate complex reveals how the universally conserved LPXTG sorting signal is recognized (English)

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2 February 2020

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Staphylococcus aureus

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2 February 2020

Robert T. Clubb

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Robert T Clubb

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2 February 2020

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Nuttee Suree

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2 February 2020

Valerie A Villareal

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2 February 2020

William Thieu

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2 February 2020

Evgeny A Fadeev

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2 February 2020

Jeremy J Clemens

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2 February 2020

Michael E Jung

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10 July 2009

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2 February 2020

Journal of Biological Chemistry

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2 February 2020

284

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2 February 2020

36

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2 February 2020

24465-24477

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2 February 2020

Sortases and the art of anchoring proteins to the envelopes of gram-positive bacteria

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Activation of Inhibitors by Sortase Triggers Irreversible Modification of the Active Site

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Protein NMR structure determination with automated NOE-identification in the NOESY spectra using the new software ATNOS

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Backbone dynamics of Escherichia coli ribonuclease HI: correlations with structure and function in an active enzyme

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Mutagenesis studies of substrate recognition and catalysis in the sortase A transpeptidase from Staphylococcus aureus

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Sortase as a target of anti-infective therapy

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Covalent attachment of proteins to solid supports and surfaces via Sortase-mediated ligation

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28 September 2017

Staphylococcus aureus Sortase A transpeptidase. Calcium promotes sorting signal binding by altering the mobility and structure of an active site loop.

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Structures of sortase B from Staphylococcus aureus and Bacillus anthracis reveal catalytic amino acid triad in the active site

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Site-specific protein modification on living cells catalyzed by Sortase

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Sortase from Staphylococcus aureus does not contain a thiolate-imidazolium ion pair in its active site

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12 December 2020

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2 February 2020

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2 February 2020

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