Sandbox 124: Difference between revisions

Line 1:

== Your Heading Here (maybe something like 'Structure') ==

Anything in this section will appear adjacent to the 3D structure and will be scrollable.

===Introduction>

'''Transpeptidases (TP), also known as penicillin-binding proteins (PBP),

catalyze the cross-linking of peptidoglycan polymers during bacterial cell wall

synthesis. The natural transpeptidase substrate is the D-Ala-D-Ala

peptidoglycan side chain terminus. Beta-lactam (β-lactam) antibiotics, which

include penicillins, cephalosporins and carbapenems, bind and irreversibly

inhibit transpeptidases by mimicking the D-Ala-D-Ala substrate, resulting in

the inhibition of cell wall synthesis and ultimately bacterial cell growth.

Overuse and misuse of β-lactams has led to the generation of methicillinresistant

Staphylococcus aureus (MRSA) isolates that have acquired an

alternative transpeptidase, PBP2a, which is neither bound nor inhibited by β-

lactams. MRSA isolates are resistant to all β-lactams, can be hospital- or

community-acquired, and are often the cause of significant morbidity and

mortality. Furthermore, they are often only susceptible to “last resort

antibiotics”, such as vancomycin. Recently, two cephalosporins - ceftobiprole

and ceftaroline - that bind and inhibit PBP2a have been developed. The

Hostos-Lincoln Academy Students Modeling A Research Topic (SMART)

Team generated a model of the PBP2a/ceftobiprole complex (PDB 4DKI)

using 3D printing technology to illustrate the mechanism of action of

ceftobiprole. Supported by a grant from the Camille and Henry Dreyfus Foundation.'''

Sandbox 124: Difference between revisions

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
+== Your Heading Here (maybe something like 'Structure') ==
+<StructureSection load='4dki' size='350' side='right' caption='Structure of HMG-CoA reductase (PDB entry [[1dq8]])' scene=''>
+Anything in this section will appear adjacent to the 3D structure and will be scrollable.
+===Introduction>
+'''Transpeptidases (TP), also known as penicillin-binding proteins (PBP),
+catalyze the cross-linking of peptidoglycan polymers during bacterial cell wall
+synthesis. The natural transpeptidase substrate is the D-Ala-D-Ala
+peptidoglycan side chain terminus. Beta-lactam (β-lactam) antibiotics, which
+include penicillins, cephalosporins and carbapenems, bind and irreversibly
+inhibit transpeptidases by mimicking the D-Ala-D-Ala substrate, resulting in
+the inhibition of cell wall synthesis and ultimately bacterial cell growth.
+Overuse and misuse of β-lactams has led to the generation of methicillinresistant
+Staphylococcus aureus (MRSA) isolates that have acquired an
+alternative transpeptidase, PBP2a, which is neither bound nor inhibited by β-
+lactams. MRSA isolates are resistant to all β-lactams, can be hospital- or
+community-acquired, and are often the cause of significant morbidity and
+mortality. Furthermore, they are often only susceptible to “last resort
+antibiotics”, such as vancomycin. Recently, two cephalosporins - ceftobiprole
+and ceftaroline - that bind and inhibit PBP2a have been developed. The
+Hostos-Lincoln Academy Students Modeling A Research Topic (SMART)
+Team generated a model of the PBP2a/ceftobiprole complex (PDB 4DKI)
+using 3D printing technology to illustrate the mechanism of action of
+ceftobiprole. Supported by a grant from the Camille and Henry Dreyfus Foundation.'''