Fluctuations in nuclear envelope's potential mediate synchronization of early neural activity |
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Authors: | Yamashita Masayuki |
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Affiliation: | aInstitut de Biologie Structurale, Bacterial Pathogenesis Group, UMR 5075 (CEA, CNRS, Univ. Joseph Fourier-Grenoble I) Grenoble, France;bICSN, CNRS UPR 2301, 91198 Gif-sur-Yvette Cedex, France;cIMPMC, CNRS UMR 7590 4 place Jussieu, 75252 Paris Cedex, France;dIMPMC, UPMC UMR 7590 4 place Jussieu, 75252 Paris Cedex, France;eSynchrotron SOLEIL, BP 48, 91192 Gif-sur-Yvette Cedex, France;fIBBMC, Université Paris Sud CNRS UMR8619, bât. 430, F-91405 Orsay Cedex, France |
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Abstract: | Penicillin binding proteins (PBPs) catalyze essential steps in the biosynthesis of peptidoglycan, the main component of the bacterial cell wall. PBPs can harbor two catalytic domains, namely the glycosyltransferase (GT) and transpeptidase (TP) activities, the latter being the target for β-lactam antibiotics. Despite the availability of structural information regarding bi-functional PBPs, little is known regarding the interaction and flexibility between the TP and GT domains. Here, we describe the structural characterization in solution by small angle X-ray scattering (SAXS) of PBP1b, a bi-functional PBP from Streptococcus pneumoniae. The molecule is present in solution as an elongated monomer. Refinement of internal coordinates starting from a homology model yields models in which the two domains are in an extended conformation without any mutual contact compatible with the existence of restricted mobility. |
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Keywords: | Penicillin binding protein Glycosyltransferase Small angle X-ray scattering Bacterial pathogenesis |
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