Sandbox 126: Difference between revisions
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== Structure of a Resistant Transpeptidase == | == Structure of a Resistant Transpeptidase == | ||
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:<scene name='37/372726/Tp_and_npb_domain/ | 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:<scene name='37/372726/Tp_and_npb_domain/3'>a non-penicillin binding (NPB) domain and a TP domain</scene> . 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 <scene name='37/372726/Close_up_of_active_site/8'>active site</scene> contains a serine residue at position | ||
<scene name='37/372726/Ser403_no_backbone/1'>403</scene> (Ser403)which catalyzes the cross-linking of the peptidoglycan rows with pentaglycine cross-links. | <scene name='37/372726/Ser403_no_backbone/1'>403</scene> (Ser403)which catalyzes the cross-linking of the peptidoglycan rows with pentaglycine cross-links. | ||
<scene name='37/372726/Tp_and_npb_domain/3'>a non-penicillin binding (NPB) domain and a TP domain</scene> | |||
== Catalytic Mechanism of PBP2a == | == Catalytic Mechanism of PBP2a == | ||
