5K9Y

Crystal structure of a thermophilic xylanase A from Bacillus subtilis 1A1 quadruple mutant Q7H/G13R/S22P/S179C

5K9Y の概要

• エントリーDOI: 10.2210/pdb5k9y/pdb
• 分子名称: Endo-1,4-beta-xylanase A (2 entities in total)
• 機能のキーワード: glycoside hydrolase family 11, endo-1, 4-beta-xylanase a, thermostability, hydrolase
• 由来する生物種: Bacillus subtilis (strain 168)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 41094.48

構造登録者

Pinheiro, M.P.,Ferreira, T.L.,Silva, S.R.B.,Fuzo, C.A.,Silva, S.R.,Lourenzoni, M.R.,Vieira, D.S.,Ward, R.J.,Nonato, M.C. (登録日: 2016-06-01, 公開日: 2017-04-12, 最終更新日: 2023-09-27)

主引用文献

Silva, S.B.,Pinheiro, M.P.,Fuzo, C.A.,Silva, S.R.,Ferreira, T.L.,Lourenzoni, M.R.,Nonato, M.C.,Vieira, D.S.,Ward, R.J.
The role of local residue environmental changes in thermostable mutants of the GH11 xylanase from Bacillus subtilis.
Int. J. Biol. Macromol., 97:574-584, 2017

PubMed Abstract: A thermostable variant of the mesophilic xylanase A from Bacillus subtilis (BsXynA-G3_4x) contains the four mutations Gln7His, Gly13Arg, Ser22Pro, and Ser179Cys. The crystal structure of the BsXynA-G3_4x has been solved, and the local environments around each of these positions investigated by molecular dynamics (MD) simulations at 328K and 348K. The structural and MD simulation results were correlated with thermodynamic data of the wild-type enzyme, the 4 single mutants and the BsXynA-G3_4x. This analysis suggests that the overall stabilizing effect is entropic, and is consistent with solvation of charged residues and reduction of main-chain flexibility. Furthermore, increased protein-protein hydrogen bonding and hydrophobic interactions also contribute to stabilize the BsXynA-G3_4x. The study revealed that a combination of several factors is responsible for increased thermostability of the BsXynA-G3_4x; (i) introduction of backbone rigidity in regions of high flexibility, (ii) solvation effects and (iii) hydrophobic contacts.

PubMed: 28109807
DOI: 10.1016/j.ijbiomac.2017.01.054

実験手法

X-RAY DIFFRACTION (2.2 Å)