PDBsum entry 3vsl

Penicillin-binding protein

PDB id: 3vsl

Contents

Protein chains

631 a.a.

Ligands

CEF ×2

Waters ×256

PDB id:

3vsl

Name:

Penicillin-binding protein

Title:

Crystal structure of penicillin-binding protein 3 (pbp3) from methicilin-resistant staphylococcus aureus in the cefotaxime bound form.

Structure:

Penicillin-binding protein 3. Chain: a, b. Engineered: yes

Source:

Staphylococcus aureus. Organism_taxid: 196620. Strain: mw2. Gene: pbp3, mw1504. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.40Å R-factor: 0.250 R-free: 0.316

Authors:

H.Yoshida,J.R.Tame,S.Y.Park

Key ref:

H.Yoshida et al. (2012). 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. PubMed id: 22846910

Date:

25-Apr-12 Release date: 31-Oct-12

Protein chains

A0A0H3K0B9  (A0A0H3K0B9_STAAW) -  Penicillin-binding protein 3 from Staphylococcus aureus (strain MW2)

Seq: 691 a.a.

Struc: 631 a.a.

J Mol Biol 423:351-364 (2012)

PubMed id: 22846910

Crystal structures of penicillin-binding protein 3 (PBP3) from methicillin-resistant Staphylococcus aureus in the apo and cefotaxime-bound forms.

H.Yoshida, F.Kawai, E.Obayashi, S.Akashi, D.I.Roper, J.R.Tame, S.Y.Park.

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.