Sandbox 22222: Difference between revisions
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Methicillin resistant Staphylococcus aureus (MRSA) is resistant to all β-lactams because it acquires an alternative PBP, PBP2a, that is not bound or inhibited by any β-lactams. PBP2a is composed of two domains: a <font color='orange'><b>non-penicillin binding domain </b><scene name='36/365380/4dki_cartoon/20'>(NPB) </scene></font> and a <font color='dodgerblue'><b>transpeptidase <scene name='36/365380/4dki_cartoon/21'>(TP)</scene> binding domain </b></font>. The NBP domain of PBP2a is anchored in the cell membrane, while the TP domain “sits” in the periplasm with its active site facing the inner surface of the cell wall. The active site contains <scene name='36/365380/Ser403/19'>a serine residue at position 403 (ser403)</scene> which catalyzes the cross-linking of the peptidoglycan rows with pentaglycine cross-links. | Methicillin resistant Staphylococcus aureus (MRSA) is resistant to all β-lactams because it acquires an alternative PBP, PBP2a, that is not bound or inhibited by any β-lactams. PBP2a is composed of two domains: a <font color='orange'><b>non-penicillin binding domain </b><scene name='36/365380/4dki_cartoon/20'>(NPB) </scene></font> and a <font color='dodgerblue'><b>transpeptidase <scene name='36/365380/4dki_cartoon/21'>(TP)</scene> binding domain </b></font>. The NBP domain of PBP2a is anchored in the cell membrane, while the TP domain “sits” in the periplasm with its active site facing the inner surface of the cell wall. The active site contains <scene name='36/365380/Ser403/19'>a serine residue at position 403 (ser403)</scene> which catalyzes the cross-linking of the peptidoglycan rows with pentaglycine cross-links. | ||
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<scene name='37/372724/Medicine_interaction/1'>ceftobiprole</scene> | <scene name='37/372724/Medicine_interaction/1'>ceftobiprole</scene> | ||
<scene name='37/372724/R2_interaction/6'>tighter binding</scene> | <scene name='37/372724/R2_interaction/6'>tighter binding</scene> | ||
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