Structural highlights
2xr0 is a 1 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
|
| Ligands: | |
| Related: | 1iyp, 1we4, 2wyx, 1iys, 1iyo, 1bza, 1iyq, 2xqz |
| Activity: | Beta-lactamase, with EC number 3.5.2.6 |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[BLT1_ECOLX] Has strong cefotaxime-hydrolyzing activity.
Publication Abstract from PubMed
Room temperature neutron diffraction data of the fully perdeuterated Toho-1 R274N/R276N double mutant beta-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 beta-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 beta-lactamase reaction pathway.
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.,Tomanicek SJ, Wang KK, Weiss KL, Blakeley MP, Cooper J, Chen Y, Coates L FEBS Lett. 2010 Dec 17. PMID:21168411[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Tomanicek SJ, Wang KK, Weiss KL, Blakeley MP, 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. 2010 Dec 17. PMID:21168411 doi:10.1016/j.febslet.2010.12.017
