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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='37/372724/non_penicillin_binding/1'>non penicillin binding</scene> (NPB) domain and a <scene name='37/372724/Transpeptidase_domain/1'>TP</scene> domain. 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 a serine residue at position 403 (<scene name='37/372724/Serine403label/2'>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:  
<scene name='37/372724/Non_penicillin_binding/1'>TextToBeDisplayed</scene> (NPB) domain and a <scene name='37/372724/Transpeptidase_domain/1'>TP</scene> domain. 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 a serine residue at position 403 (<scene name='37/372724/Serine403label/2'>Ser403</scene>)which catalyzes the cross-linking of the peptidoglycan rows with pentaglycine cross-links.




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Wayne Decatur, Student, Allison Granberry, Marisa L. VanBrakle