We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

Sandbox 126

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 2: Line 2:
==Background==
==Background==
-
PBP2a is composed of two domains: a non-penicillin binding ('''NPB''') domain and a '''TP''' 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 ('''Ser403''') which catalyzes the cross-linking of the peptidoglycan rows with pentaglycine cross-links.
+
PBP2a is composed of two domains: a '''non-penicillin binding''' (NPB) domain and a '''TP''' 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 ('''Ser403''') which catalyzes the cross-linking of the peptidoglycan rows with pentaglycine cross-links.
<scene name='37/372726/Pbp2a/1'>PBP2a resticted *b</scene>
<scene name='37/372726/Pbp2a/1'>PBP2a resticted *b</scene>
==Catalytic Mechanism of PBP2a==
==Catalytic Mechanism of PBP2a==

Revision as of 19:15, 23 July 2013

Structure of PBP2a

Drag the structure with the mouse to rotate

Background

PBP2a is composed of two domains: a non-penicillin binding (NPB) domain and a TP 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 (Ser403) which catalyzes the cross-linking of the peptidoglycan rows with pentaglycine cross-links.

Catalytic Mechanism of PBP2a

Personal tools