3VSK

Crystal structure of penicillin-binding protein 3 (PBP3) from methicilin-resistant Staphylococcus aureus in the apo form.

Summary for 3VSK

• Entry DOI: 10.2210/pdb3vsk/pdb
• Related: 3VSL
• Descriptor: Penicillin-binding protein 3 (2 entities in total)
• Functional Keywords: penicillin-binding domain, transpeptidase, penicillin-binding protein
• Biological source: Staphylococcus aureus
• Total number of polymer chains: 2
• Total formula weight: 144269.47

Authors

Yoshida, H.,Tame, J.R.,Park, S.Y. (deposition date: 2012-04-25, release date: 2012-10-31, Last modification date: 2024-03-20)

Primary citation

Yoshida, H.,Kawai, F.,Obayashi, E.,Akashi, S.,Roper, D.I.,Tame, J.R.,Park, S.Y.
Crystal Structures of Penicillin-Binding Protein 3 (PBP3) from Methicillin-Resistant Staphylococcus aureus in the Apo and Cefotaxime-Bound Forms.
J.Mol.Biol., 423:351-364, 2012

PubMed Abstract: Staphylococcus aureus is a widespread Gram-positive opportunistic pathogen, and a methicillin-resistant form (MRSA) is particularly difficult to treat clinically. We have solved two crystal structures of penicillin-binding protein (PBP) 3 (PBP3) from MRSA, the apo form and a complex with the β-lactam antibiotic cefotaxime, and used electrospray mass spectrometry to measure its sensitivity to a variety of penicillin derivatives. PBP3 is a class B PBP, possessing an N-terminal non-penicillin-binding domain, sometimes called a dimerization domain, and a C-terminal transpeptidase domain. The model shows a different orientation of its two domains compared to earlier models of other class B PBPs and a novel, larger N-domain. Consistent with the nomenclature of "dimerization domain", the N-terminal region forms an apparently tight interaction with a neighboring molecule related by a 2-fold symmetry axis in the crystal structure. This dimer form is predicted to be highly stable in solution by the PISA server, but mass spectrometry and analytical ultracentrifugation provide unequivocal evidence that the protein is a monomer in solution.

PubMed: 22846910
DOI: 10.1016/j.jmb.2012.07.012

Experimental method

X-RAY DIFFRACTION (2.301 Å)