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)''' | + | {{Structure |
| + | |PDB= 1pmd |SIZE=350|CAPTION= <scene name='initialview01'>1pmd</scene>, resolution 3.5Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''PENICILLIN-BINDING PROTEIN 2X (PBP-2X)''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1PMD is a [ | + | 1PMD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_pneumoniae Streptococcus pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PMD OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8605631 8605631] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Streptococcus pneumoniae]] | [[Category: Streptococcus pneumoniae]] | ||
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[[Category: transmembrane]] | [[Category: transmembrane]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:26:11 2008'' |
Revision as of 11:26, 20 March 2008
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| 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
Page seeded by OCA on Thu Mar 20 13:26:11 2008
