Sandbox 127: Difference between revisions

Line 30:

== Structure of PBP2a, a B-lactam Resistant Transpeptidase==

Isolates of methicillin-resistant S. aureus (MRSA) are resistant to almost all currently available B-lactam because they have acquired an alternative PBP, PBP2a(encoded by the mecA gene), that is neither bound nor inhibited by B-lactams. PBP2a is composed of two domains:a a non-penicillin binding domain <scene name='36/365380/4dki_cartoon/17'>(NPB) </scene> and a transpeptidase <scene name='36/365380/4dki_cartoon/18'>(TP)</scene> binding domain . The NPB domain of PBP2a is anchored in the cell membrane, while the TP domain resides 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 (Ser403) which catalyzes the cross-linking of the peptidoglycan rows with pentaglycine cross-links.

Isolates of methicillin-resistant S. aureus (MRSA) are resistant to almost all currently available B-lactam because they have acquired an alternative PBP, PBP2a(encoded by the mecA gene), that is neither bound nor inhibited by B-lactams. PBP2a is composed of two domains:a a non-penicillin binding domain <scene name='36/365380/4dki_cartoon/17'>(NPB) </scene> and a transpeptidase <scene name='36/365380/4dki_cartoon/18'>(TP)</scene> binding domain . The NPB domain of PBP2a is anchored in the cell membrane, while the TP domain resides in the periplasm with its active site facing the inner surface of the cell wall. The active site contains <scene name='36/365380/Ser403/15'> at position 403 (Ser403) which catalyzes the cross-linking of the peptidoglycan rows with pentaglycine cross-links.

Sandbox 127: Difference between revisions

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

Revision as of 21:20, 18 September 2013 view source Allison Granberry (talk \| contribs) 742 edits No edit summary ← Older edit		Revision as of 21:22, 18 September 2013 view source Allison Granberry (talk \| contribs) 742 edits No edit summary Newer edit →
Line 30:		Line 30:
	== Structure of PBP2a, a B-lactam Resistant Transpeptidase==		== Structure of PBP2a, a B-lactam Resistant Transpeptidase==

	Isolates of methicillin-resistant S. aureus (MRSA) are resistant to almost all currently available B-lactam because they have acquired an alternative PBP, PBP2a(encoded by the mecA gene), that is neither bound nor inhibited by B-lactams. PBP2a is composed of two domains:a a <font color='orange'><b>non-penicillin binding domain </b><scene name='36/365380/4dki_cartoon/17'>(NPB) </scene></font> and a <font color='dodgerblue'><b>transpeptidase <scene name='36/365380/4dki_cartoon/18'>(TP)</scene> binding domain </b></font>. The NPB domain of PBP2a is anchored in the cell membrane, while the TP domain resides 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 (Ser403) which catalyzes the cross-linking of the peptidoglycan rows with pentaglycine cross-links.		Isolates of methicillin-resistant S. aureus (MRSA) are resistant to almost all currently available B-lactam because they have acquired an alternative PBP, PBP2a(encoded by the mecA gene), that is neither bound nor inhibited by B-lactams. PBP2a is composed of two domains:a a <font color='orange'><b>non-penicillin binding domain </b><scene name='36/365380/4dki_cartoon/17'>(NPB) </scene></font> and a <font color='dodgerblue'><b>transpeptidase <scene name='36/365380/4dki_cartoon/18'>(TP)</scene> binding domain </b></font>. The NPB domain of PBP2a is anchored in the cell membrane, while the TP domain resides in the periplasm with its active site facing the inner surface of the cell wall. The active site contains <scene name='36/365380/Ser403/15'> at position 403 (Ser403) which catalyzes the cross-linking of the peptidoglycan rows with pentaglycine cross-links.