1mwt: Difference between revisions
No edit summary |
No edit summary |
||
Line 1: | Line 1: | ||
[[Image:1mwt.jpg|left|200px]] | [[Image:1mwt.jpg|left|200px]] | ||
<!-- | |||
The line below this paragraph, containing "STRUCTURE_1mwt", creates the "Structure Box" on the page. | |||
You may change the PDB parameter (which sets the PDB file loaded into the applet) | |||
or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |||
| | or leave the SCENE parameter empty for the default display. | ||
| | --> | ||
{{STRUCTURE_1mwt| PDB=1mwt | SCENE= }} | |||
}} | |||
'''Structure of penicillin G acyl-Penicillin binding protein 2a from methicillin resistant Staphylococcus aureus strain 27r at 2.45 A resolution.''' | '''Structure of penicillin G acyl-Penicillin binding protein 2a from methicillin resistant Staphylococcus aureus strain 27r at 2.45 A resolution.''' | ||
Line 27: | Line 24: | ||
[[Category: Lim, D C.]] | [[Category: Lim, D C.]] | ||
[[Category: Strynadka, N C.J.]] | [[Category: Strynadka, N C.J.]] | ||
[[Category: | [[Category: Beta-lactam]] | ||
[[Category: | [[Category: D,d-carboxypeptidase]] | ||
[[Category: | [[Category: D,d-transpeptidase]] | ||
[[Category: | [[Category: Penicillin binding protein]] | ||
[[Category: | [[Category: Penicillin g]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 01:48:58 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on |
Revision as of 01:49, 3 May 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. 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 Sat May 3 01:48:58 2008