Aminoglycoside Acetlytransferases were first identified in Serratia marcescens in the 1960s and later crystallized in 1998, revealing key details about the structure and function of acetyltransferases. S. marcescens is a gram-negative bacteria that is known to cause UTIs, pneumonia, and sepsis. Aminoglycoside antibiotics, such as Sisomicin are used to treat these conditions by inactivating the bacterias’ ribosome. Antibiotic resistance and the growing danger of superbugs among bacterial infections combined with the lack of new antibiotic developments, indicates a need to better understand how proteins that confer antibiotic resistance to bacteria can circumvent our current treatment options.
This is a default text for your page Aleena Ahmad/Sandbox 1. Click above on edit this page to modify. Be careful with the < and > signs. You may include any references to papers as in: the use of JSmol in Proteopedia [1] or to the article describing Jmol [2] to the rescue. 5'N to 3'C rainbow colouring of Protein Spermidine and Catalytic Base Asp147 Acetyl CoA and Catalytic Acids Arg118 and Arg119 ContentsIntroductionGNAT SuperfamilyConserved Motifs
FunctionMechanismStructures of ImportanceC-terminalPossible Catalytic ResiduesImportance of DimerDiseaseRelevanceThis is a sample scene created with SAT to color by Group, and another to make a transparent representation of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
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This page was last modified 16:47, 24 April 2026.
