Structural highlights
Function
BLT1_ECOLX Has strong cefotaxime-hydrolyzing activity.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The beta-lactamase Toho-1 exhibits a strong tendency to form merohedrally twinned crystals. Here, the crystal quality of Toho-1 was improved by using surface modification to remove a sulfate ion involved in crystal packing. The surface-modified Toho-1 variant (R274N/R276N) was crystallized under similar conditions to those used for wild-type Toho-1. R274N/R276N did not form merohedrally twinned crystals. The crystals diffracted to a significantly higher resolution (approximately 0.97 A) than the wild-type crystals (1.65 A); they belonged to the same space group and had almost identical unit-cell parameters to those of wild-type Toho-1.
Improvement of crystal quality by surface mutations of beta-lactamase Toho-1.,Shimamura T, Nitanai Y, Uchiyama T, Matsuzawa H Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Apr 1;65(Pt, 4):379-82. Epub 2009 Mar 25. PMID:19342785[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Shimamura T, Nitanai Y, Uchiyama T, Matsuzawa H. Improvement of crystal quality by surface mutations of beta-lactamase Toho-1. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Apr 1;65(Pt, 4):379-82. Epub 2009 Mar 25. PMID:19342785 doi:S1744309109008240
