1pmd: Difference between revisions

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[[Image:1pmd.gif|left|200px]]<br /><applet load="1pmd" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1pmd.gif|left|200px]]<br /><applet load="1pmd" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1pmd, resolution 3.5Å" />

'''PENICILLIN-BINDING PROTEIN 2X (PBP-2X)'''<br />

==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.

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 [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://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1PMD OCA].

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==

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[[Category: transmembrane]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20 23~~:55:~~23 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:30:15 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1pmd.gif|left|200px]]<br /><applet load="1pmd" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1pmd.gif|left|200px]]<br /><applet load="1pmd" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1pmd, resolution 3.5&Aring;" />
 '''PENICILLIN-BINDING PROTEIN 2X (PBP-2X)'''<br />
 ==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.
+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==
-PMD 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PMD OCA].
+PMD 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==
@@ Line 21: / Line 21: @@
 [[Category: transmembrane]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:55:23 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:30:15 2008''