 |
PDBsum entry 1pmd
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Peptidoglycan synthesis
|
PDB id
|
|
|
|
1pmd
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
X-Ray structure of streptococcus pneumoniae pbp2X, A primary penicillin target enzyme.
|
|
|
Authors
|
|
S.Pares,
N.Mouz,
Y.Pétillot,
R.Hakenbeck,
O.Dideberg.
|
|
|
Ref.
|
|
Nat Struct Biol, 1996,
3,
284-289.
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
All beta-lactam antibiotics exert their biological effects by interacting with a
unique class of proteins, the penicillin-binding proteins (PBPs). These membrane
proteins are involved in the biosynthesis of the murein or peptidoglycan, a
mesh-like structure which completely surrounds the bacterial cell. Sequence
similarities indicate that one domain of these proteins belongs to a large
family of beta-lactam-recognizing proteins, which includes the active-site
serine beta-lactamases. We here report the first three-dimensional crystal
structure of a high molecular weight penicillin-binding protein, PBP2x of
Streptococcus pneumoniae, at 3.5 A resolution. The molecule has three domains,
the central domain being a transpeptidase, which is a suitable target for
antibiotic development.
|
|
|
Secondary reference #1
|
|
|
Title
|
|
Crystallization of a genetically engineered water-Soluble primary penicillin target enzyme. The high molecular mass pbp2X of streptococcus pneumoniae.
|
|
|
Authors
|
|
P.Charlier,
G.Buisson,
O.Dideberg,
J.Wierenga,
W.Keck,
G.Laible,
R.Hakenbeck.
|
|
|
Ref.
|
|
J Mol Biol, 1993,
232,
1007-1009.
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Headers
|
|
|
|
|
|
