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

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Yoshida, Hisashi, Kawai, Fumihiro, Obayashi, Eiji, Akashi, Satoko, Roper, David I., Tame, Jeremy R.H. and Park, Sam-Yong (2012) Crystal structures of penicillin-binding protein 3 (PBP3) from methicillin-resistant staphylococcus aureus in the apo and cefotaxime‐bound forms. Journal of Molecular Biology, Volume 423 (Number 3). pp. 351-364. doi:10.1016/j.jmb.2012.07.012 ISSN 0022-2836.

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Official URL: http://dx.doi.org/10.1016/j.jmb.2012.07.012

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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.

Item Type: Journal Article
Divisions: Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- )
Journal or Publication Title: Journal of Molecular Biology
Publisher: Academic Press
ISSN: 0022-2836
Official Date: 26 October 2012
Dates:
DateEvent
26 October 2012Published
Volume: Volume 423
Number: Number 3
Page Range: pp. 351-364
DOI: 10.1016/j.jmb.2012.07.012
Status: Peer Reviewed
Publication Status: Published
Access rights to Published version: Restricted or Subscription Access

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