1pmd
From Proteopedia
(New page: 200px<br /><applet load="1pmd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pmd, resolution 3.5Å" /> '''PENICILLIN-BINDING PR...) |
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| - | [[Image:1pmd.gif|left|200px]]<br /><applet load="1pmd" size=" | + | [[Image:1pmd.gif|left|200px]]<br /><applet load="1pmd" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1pmd, resolution 3.5Å" /> | caption="1pmd, resolution 3.5Å" /> | ||
'''PENICILLIN-BINDING PROTEIN 2X (PBP-2X)'''<br /> | '''PENICILLIN-BINDING PROTEIN 2X (PBP-2X)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | All beta-lactam antibiotics exert their biological effects by interacting | + | 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== | ==About this Structure== | ||
| - | 1PMD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_pneumoniae Streptococcus pneumoniae]. Full crystallographic information is available from [http:// | + | 1PMD is a [http://en.wikipedia.org/wiki/Single_protein 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== | ||
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[[Category: transmembrane]] | [[Category: transmembrane]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:30:15 2008'' |
Revision as of 12:30, 21 February 2008
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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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