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1pmd
From Proteopedia
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[[Image:1pmd.gif|left|200px]] | [[Image:1pmd.gif|left|200px]] | ||
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'''PENICILLIN-BINDING PROTEIN 2X (PBP-2X)''' | '''PENICILLIN-BINDING PROTEIN 2X (PBP-2X)''' | ||
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[[Category: Mouz, N.]] | [[Category: Mouz, N.]] | ||
[[Category: Pares, S.]] | [[Category: Pares, S.]] | ||
| - | [[Category: | + | [[Category: Cell wall]] |
| - | [[Category: | + | [[Category: Peptidoglycan synthesis]] |
| - | [[Category: | + | [[Category: Resistance]] |
| - | [[Category: | + | [[Category: Transmembrane]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:14:52 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 02:14, 3 May 2008
PENICILLIN-BINDING PROTEIN 2X (PBP-2X)
Overview
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.
About this Structure
1PMD is a Single protein structure of sequence from Streptococcus pneumoniae. Full crystallographic information is available from OCA.
Reference
X-ray structure of Streptococcus pneumoniae PBP2x, a primary penicillin target enzyme., Pares S, Mouz N, Petillot Y, Hakenbeck R, Dideberg O, Nat Struct Biol. 1996 Mar;3(3):284-9. PMID:8605631 Page seeded by OCA on Sat May 3 05:14:52 2008
