2XR0
Room temperature X-ray structure of the perdeuterated Toho-1 R274N R276N double mutant beta-lactamase
Summary for 2XR0
| Entry DOI | 10.2210/pdb2xr0/pdb |
| Related | 1BZA 1IYO 1IYP 1IYQ 1IYS 1WE4 2WYX 2XQZ |
| Descriptor | TOHO-1 BETA-LACTAMASE, SULFATE ION (3 entities in total) |
| Functional Keywords | hydrolase, extended-spectrum beta-lactamases, esbls, ctx-m-type esbls |
| Biological source | ESCHERICHIA COLI |
| Total number of polymer chains | 1 |
| Total formula weight | 28278.80 |
| Authors | Tomanicek, S.J.,Wang, K.K.,Weiss, K.L.,Blakeley, M.P.,Cooper, J.,Chen, Y.,Coates, L. (deposition date: 2010-09-08, release date: 2010-12-22, Last modification date: 2023-12-20) |
| Primary citation | Tomanicek, S.J.,Wang, K.K.,Weiss, K.L.,Blakeley, M.P.,Cooper, J.,Chen, Y.,Coates, L. The 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. FEBS Lett., 585:364-, 2011 Cited by PubMed Abstract: Room temperature neutron diffraction data of the fully perdeuterated Toho-1 R274N/R276N double mutant β-lactamase in the apo form were used to visualize deuterium atoms within the active site of the enzyme. This perdeuterated neutron structure of the Toho-1 R274N/R276N reveals the clearest picture yet of the ground-state active site protonation states and the complete hydrogen-bonding network in a β-lactamase enzyme. The ground-state active site protonation states detailed in this neutron diffraction study are consistent with previous high-resolution X-ray studies that support the role of Glu166 as the general base during the acylation reaction in the class A β-lactamase reaction pathway. PubMed: 21168411DOI: 10.1016/J.FEBSLET.2010.12.017 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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