1mwt: Difference between revisions

Revision as of 14:59, 21 February 2008

Structure of penicillin G acyl-Penicillin binding protein 2a from methicillin resistant Staphylococcus aureus strain 27r at 2.45 A resolution.

OverviewOverview

The multiple antibiotic resistance of methicillin-resistant strains of Staphylococcus aureus (MRSA) has become a major clinical problem worldwide. The key determinant of the broad-spectrum beta-lactam resistance in MRSA strains is the penicillin-binding protein 2a (PBP2a). Because of its low affinity for beta-lactams, PBP2a provides transpeptidase activity to allow cell wall synthesis at beta-lactam concentrations that inhibit the beta-lactam-sensitive PBPs normally produced by S. aureus. The crystal structure of a soluble derivative of PBP2a has been determined to 1.8 A resolution and provides the highest resolution structure for a high molecular mass PBP. Additionally, structures of the acyl-PBP complexes of PBP2a with nitrocefin, penicillin G and methicillin allow, for the first time, a comparison of an apo and acylated resistant PBP. An analysis of the PBP2a active site in these forms reveals the structural basis of its resistance and identifies features in newly developed beta-lactams that are likely important for high affinity binding.

About this StructureAbout this Structure

1MWT is a Single protein structure of sequence from Staphylococcus aureus with and as ligands. Full crystallographic information is available from OCA.

ReferenceReference

Structural basis for the beta lactam resistance of PBP2a from methicillin-resistant Staphylococcus aureus., Lim D, Strynadka NC, Nat Struct Biol. 2002 Nov;9(11):870-6. PMID:12389036

Page seeded by OCA on Thu Feb 21 13:59:51 2008

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OCA

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-[[Image:1mwt.jpg|left|200px]]<br /><applet load="1mwt" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1mwt.jpg|left|200px]]<br /><applet load="1mwt" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1mwt, resolution 2.45&Aring;" />
 '''Structure of penicillin G acyl-Penicillin binding protein 2a from methicillin resistant Staphylococcus aureus strain 27r at 2.45 A resolution.'''<br />
 ==Overview==
-The multiple antibiotic resistance of methicillin-resistant strains of, Staphylococcus aureus (MRSA) has become a major clinical problem, worldwide. The key determinant of the broad-spectrum beta-lactam, resistance in MRSA strains is the penicillin-binding protein 2a (PBP2a)., Because of its low affinity for beta-lactams, PBP2a provides, transpeptidase activity to allow cell wall synthesis at beta-lactam, concentrations that inhibit the beta-lactam-sensitive PBPs normally, produced by S. aureus. The crystal structure of a soluble derivative of, PBP2a has been determined to 1.8 A resolution and provides the highest, resolution structure for a high molecular mass PBP. Additionally, structures of the acyl-PBP complexes of PBP2a with nitrocefin, penicillin, G and methicillin allow, for the first time, a comparison of an apo and, acylated resistant PBP. An analysis of the PBP2a active site in these, forms reveals the structural basis of its resistance and identifies, features in newly developed beta-lactams that are likely important for, high affinity binding.
+The multiple antibiotic resistance of methicillin-resistant strains of Staphylococcus aureus (MRSA) has become a major clinical problem worldwide. The key determinant of the broad-spectrum beta-lactam resistance in MRSA strains is the penicillin-binding protein 2a (PBP2a). Because of its low affinity for beta-lactams, PBP2a provides transpeptidase activity to allow cell wall synthesis at beta-lactam concentrations that inhibit the beta-lactam-sensitive PBPs normally produced by S. aureus. The crystal structure of a soluble derivative of PBP2a has been determined to 1.8 A resolution and provides the highest resolution structure for a high molecular mass PBP. Additionally, structures of the acyl-PBP complexes of PBP2a with nitrocefin, penicillin G and methicillin allow, for the first time, a comparison of an apo and acylated resistant PBP. An analysis of the PBP2a active site in these forms reveals the structural basis of its resistance and identifies features in newly developed beta-lactams that are likely important for high affinity binding.
 ==About this Structure==
-MWT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus] with CD and CL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MWT OCA].
+MWT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus] with <scene name='pdbligand=CD:'>CD</scene> and <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MWT OCA].
 ==Reference==
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 [[Category: Single protein]]
 [[Category: Staphylococcus aureus]]
-[[Category: Lim, D.C.]]
+[[Category: Lim, D C.]]
-[[Category: Strynadka, N.C.J.]]
+[[Category: Strynadka, N C.J.]]
 [[Category: CD]]
 [[Category: CL]]
@@ Line 24: / Line 24: @@
 [[Category: penicillin g]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 22:08:44 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:59:51 2008''