2fff: Difference between revisions

Line 4:

==Overview==

The class A PBP1b from Streptococcus pneumoniae is responsible for, glycosyltransferase and transpeptidase (TP) reactions, forming the, peptidoglycan of the bacterial cell wall. The enzyme has been produced in, a stable, soluble form and undergoes time-dependent proteolysis to leave, an intact TP domain. Crystals of this TP domain were obtained, diffracting, to 2.2 A resolution, and the structure was solved by using molecular, replacement. Analysis of the structure revealed an "open" active site, with important conformational differences to the previously determined, "closed" apoenzyme. The active-site nucleophile, Ser460, is in an, orientation that allows for acylation by beta-lactams. Consistent with the, productive conformation of the conserved active-site catalytic residues, adjacent loops show only minor deviation from those of known acyl-enzyme, structures. These findings are discussed in the context of enzyme, functionality and the possible conformational sampling of PBP1b between, active and inactive states.

The class A PBP1b from Streptococcus pneumoniae is responsible for glycosyltransferase and transpeptidase (TP) reactions, forming the peptidoglycan of the bacterial cell wall. The enzyme has been produced in a stable, soluble form and undergoes time-dependent proteolysis to leave an intact TP domain. Crystals of this TP domain were obtained, diffracting to 2.2 A resolution, and the structure was solved by using molecular replacement. Analysis of the structure revealed an "open" active site, with important conformational differences to the previously determined "closed" apoenzyme. The active-site nucleophile, Ser460, is in an orientation that allows for acylation by beta-lactams. Consistent with the productive conformation of the conserved active-site catalytic residues, adjacent loops show only minor deviation from those of known acyl-enzyme structures. These findings are discussed in the context of enzyme functionality and the possible conformational sampling of PBP1b between active and inactive states.

==About this Structure==

Line 13:

[[Category: Protein complex]]

[[Category: Streptococcus pneumoniae]]

[[Category: Lovering, A.L.]]

[[Category: Lovering, A L.]]

[[Category: Strynadka, N.C.J.]]

[[Category: Strynadka, N C.J.]]

[[Category: NI]]

[[Category: transpeptidase fold]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Tue Jan 29 19~~:35:13 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:20:53 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 4: / Line 4: @@
 ==Overview==
-The class A PBP1b from Streptococcus pneumoniae is responsible for, glycosyltransferase and transpeptidase (TP) reactions, forming the, peptidoglycan of the bacterial cell wall. The enzyme has been produced in, a stable, soluble form and undergoes time-dependent proteolysis to leave, an intact TP domain. Crystals of this TP domain were obtained, diffracting, to 2.2 A resolution, and the structure was solved by using molecular, replacement. Analysis of the structure revealed an "open" active site, with important conformational differences to the previously determined, "closed" apoenzyme. The active-site nucleophile, Ser460, is in an, orientation that allows for acylation by beta-lactams. Consistent with the, productive conformation of the conserved active-site catalytic residues, adjacent loops show only minor deviation from those of known acyl-enzyme, structures. These findings are discussed in the context of enzyme, functionality and the possible conformational sampling of PBP1b between, active and inactive states.
+The class A PBP1b from Streptococcus pneumoniae is responsible for glycosyltransferase and transpeptidase (TP) reactions, forming the peptidoglycan of the bacterial cell wall. The enzyme has been produced in a stable, soluble form and undergoes time-dependent proteolysis to leave an intact TP domain. Crystals of this TP domain were obtained, diffracting to 2.2 A resolution, and the structure was solved by using molecular replacement. Analysis of the structure revealed an "open" active site, with important conformational differences to the previously determined "closed" apoenzyme. The active-site nucleophile, Ser460, is in an orientation that allows for acylation by beta-lactams. Consistent with the productive conformation of the conserved active-site catalytic residues, adjacent loops show only minor deviation from those of known acyl-enzyme structures. These findings are discussed in the context of enzyme functionality and the possible conformational sampling of PBP1b between active and inactive states.
 ==About this Structure==
@@ Line 13: / Line 13: @@
 [[Category: Protein complex]]
 [[Category: Streptococcus pneumoniae]]
-[[Category: Lovering, A.L.]]
+[[Category: Lovering, A L.]]
-[[Category: Strynadka, N.C.J.]]
+[[Category: Strynadka, N C.J.]]
 [[Category: NI]]
 [[Category: transpeptidase fold]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 19:35:13 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:20:53 2008''