1pmd
From Proteopedia
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|GENE= | |GENE= | ||
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| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1pmd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pmd OCA], [http://www.ebi.ac.uk/pdbsum/1pmd PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1pmd RCSB]</span> | ||
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[[Category: transmembrane]] | [[Category: transmembrane]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:01:34 2008'' |
Revision as of 20:01, 30 March 2008
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| , resolution 3.5Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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