1mwr
From Proteopedia
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|PDB= 1mwr |SIZE=350|CAPTION= <scene name='initialview01'>1mwr</scene>, resolution 2.45Å | |PDB= 1mwr |SIZE=350|CAPTION= <scene name='initialview01'>1mwr</scene>, resolution 2.45Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene> | + | |LIGAND= <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1mws|1MWS]], [[1mwt|1MWT]], [[1mwu|1MWU]], [[1mwx|1MWX]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mwr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mwr OCA], [http://www.ebi.ac.uk/pdbsum/1mwr PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1mwr RCSB]</span> | ||
}} | }} | ||
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[[Category: Lim, D C.]] | [[Category: Lim, D C.]] | ||
[[Category: Strynadka, N C.J.]] | [[Category: Strynadka, N C.J.]] | ||
| - | [[Category: CD]] | ||
| - | [[Category: CL]] | ||
[[Category: beta-lactam]] | [[Category: beta-lactam]] | ||
| - | [[Category: d | + | [[Category: d,d-carboxypeptidase]] |
| - | + | [[Category: d,d-transpeptidase]] | |
| - | [[Category: d-transpeptidase]] | + | |
[[Category: penicillin binding protein]] | [[Category: penicillin binding protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:22:13 2008'' |
Revision as of 19:22, 30 March 2008
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| , resolution 2.45Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Related: | 1MWS, 1MWT, 1MWU, 1MWX
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of SeMet Penicillin binding protein 2a from methicillin resistant Staphylococcus aureus strain 27r (trigonal form) at 2.45 A resolution.
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.
About this Structure
1MWR is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.
Reference
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
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