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TitleThe Active Site Protonation States of Perdeuterated Toho-1 Beta-Lactamase Determined by Neutron Diffraction Support a Role for Glu166 as the General Base in Acylation.
Journal, issue, pagesFEBS Lett., Vol. 585, Page 364-, Year 2011
Publish dateSep 8, 2010 (structure data deposition date)
AuthorsTomanicek, S.J. / Wang, K.K. / Weiss, K.L. / Blakeley, M.P. / Cooper, J. / Chen, Y. / Coates, L.
External linksFEBS Lett. / PubMed:21168411
Methodsneutron diffraction / X-ray diffraction
Resolution2.1 - 2.2 Å
Structure data

PDB-2xqz:
Neutron structure of the perdeuterated Toho-1 R274N R276N double mutant beta-lactamase
Method: NEUTRON DIFFRACTION / Resolution: 2.1 Å

PDB-2xr0:
Room temperature X-ray structure of the perdeuterated Toho-1 R274N R276N double mutant beta-lactamase
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

Chemicals

ChemComp-DOD:
DEUTERATED WATER

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

Source
  • escherichia coli (E. coli)
KeywordsHYDROLASE / EXTENDED-SPECTRUM BETA-LACTAMASES (ESBLS) / CTX-M-TYPE ESBLS / EXTENDED-SPECTRUM BETA-LACTAMASES / ESBLS

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