Scholarlink

<p>Endo-1,4-β-xylanase, a cell wall-degrading enzyme, plays a crucial role in the pathogenicity of <i>Botrytis cinerea</i> (a.k.a <i>Botryotinia fuckeliana</i>), a devastating plant disease that affects many crops worldwide. Targeting xylanase with potent inhibitors can effectively disrupt its function, thereby reducing the virulence of <i>B. cinerea</i>. The present study demonstrates the structural dynamics as well as inhibitory mechanisms of <i>B. cinerea</i> xylanase using computational approaches. The interactions of xylanase with its natural substrate xylohexose along with two suspected inhibitors, trimethoxy-cinnamic acid (TMC), and coniferyl alcohol (CA) were investigated using homology modeling, molecular dynamics simulations, and binding energy calculations. One microsecond molecular dynamics simulation demonstrated that the native substrate complex maintained optimum stability via a dense network of hydrogen bonds and close-range interactions. Among the inhibitors, TMC had a binding affinity (-59.628&#xa0;kJ/mol) than the natural substrate (-50.396&#xa0;kJ/mol) and more stable conformational dynamics, indicating its potential as a competitive inhibitor, while coniferyl alcohol had a similar binding energy (-49.220&#xa0;kJ/mol) as compared to its natural substrate. Principal component analysis and free energy landscape illustrated the dynamics of the protein upon ligand binding. These findings contribute to a better understanding of the xylanase inhibition processes and lays the groundwork for the rational development of new antifungal drugs that target <i>B. cinerea</i>. Given the increasing threat of fungal pathogens in agriculture, this study provides insights that could aid in the development of future biocontrol strategies for crop protection.</p>

错误：搜索内容不能为空，请输入英文关键词
错误：关键词超出字数限制，请精简
高级检索

Structural characterization of endo-β-1,4-xylanase of Botrytis cinerea and the dynamic insights into its differential inhibition mechanisms by TMC and coniferyl alcohol

  • 期刊论文

  • 发表日期：

    2025年11月26日

查看全文
  • Akanksha Kotiya,
  • Surya Pratap Singh,
  • Rajabrata Bhuyan

摘要

Endo-1,4-β-xylanase, a cell wall-degrading enzyme, plays a crucial role in the pathogenicity of Botrytis cinerea (a.k.a Botryotinia fuckeliana), a devastating plant disease that affects many crops worldwide. Targeting xylanase with potent inhibitors can effectively disrupt its function, thereby reducing the virulence of B. cinerea. The present study demonstrates the structural dynamics as well as inhibitory mechanisms of B. cinerea xylanase using computational approaches. The interactions of xylanase with its natural substrate xylohexose along with two suspected inhibitors, trimethoxy-cinnamic acid (TMC), and coniferyl alcohol (CA) were investigated using homology modeling, molecular dynamics simulations, and binding energy calculations. One microsecond molecular dynamics simulation demonstrated that the native substrate complex maintained optimum stability via a dense network of hydrogen bonds and close-range interactions. Among the inhibitors, TMC had a binding affinity (-59.628 kJ/mol) than the natural substrate (-50.396 kJ/mol) and more stable conformational dynamics, indicating its potential as a competitive inhibitor, while coniferyl alcohol had a similar binding energy (-49.220 kJ/mol) as compared to its natural substrate. Principal component analysis and free energy landscape illustrated the dynamics of the protein upon ligand binding. These findings contribute to a better understanding of the xylanase inhibition processes and lays the groundwork for the rational development of new antifungal drugs that target B. cinerea. Given the increasing threat of fungal pathogens in agriculture, this study provides insights that could aid in the development of future biocontrol strategies for crop protection.