2cnc
From Proteopedia
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FAMILY 10 XYLANASE
Overview
Thermostability is an important property of industrially significant, hydrolytic enzymes: understanding the structural basis for this attribute, will underpin the future biotechnological exploitation of these, biocatalysts. The Cellvibrio family 10 (GH10) xylanases display, considerable sequence identity but exhibit significant differences in, thermostability; thus, these enzymes represent excellent models to examine, the structural basis for the variation in stability displayed by these, glycoside hydrolases. Here, we have subjected the intracellular Cellvibrio, mixtus xylanase CmXyn10B to forced protein evolution. Error-prone PCR and, selection identified a double mutant, A334V/G348D, which confers an, increase in thermostability. The mutant has a Tm 8 degrees C higher than, the ... [(full description)]
About this Structure
2CNC is a [Single protein] structure of sequence from [Cellvibrio mixtus] with XYS, CL and MG as [ligands]. Full crystallographic information is available from [OCA].
Reference
Probing the structural basis for the difference in thermostability displayed by family 10 xylanases., Xie H, Flint J, Vardakou M, Lakey JH, Lewis RJ, Gilbert HJ, Dumon C, J Mol Biol. 2006 Jun 30;360(1):157-67. Epub 2006 May 15. PMID:16762367
Page seeded by OCA on Mon Oct 29 15:53:56 2007
Categories: Cellvibrio mixtus | Single protein | Dumon, C. | Flint, J. | Gilbert, H.J. | Lakey, J.H. | Lewis, R.J. | Vardakou, M. | Xie, H. | CL | MG | XYS | Decorated sugar | Glycosidase | Hydrolase | Thermostability | Xylan degradation | Xylanase
