STRUCTURAL DETERMINATION OF IRON CONTAINING PROTEIN BY MAD PHASING: DRUG DESIGN

纤维单胞菌fimi β-1，4-聚糖酶Cex催化结构域 Cex（cex-cd）在许多方面都是保留 β-1，4-聚糖酶，这是至关重要的， 裂解常见的β-1，4-键， 对替代能源行业的兴趣， 生物质的形式。 与Steve Withers博士合作，Tony 沃伦和他在不列颠哥伦比亚省大学的同事们， 能够研究cex-cd单独和 与酶催化机制中的中间体形成复合物。 这导致了对这种蛋白质识别的新见解， 特异性糖部分。 它还有助于解决 关于这一中间体性质的长期争论 反应：我们提供了强有力的证据支持共价键 中间模型 我们还能够确定具体的 酶和底物之间的接触， 形成反应的过渡态。

Cellulomonas fimi beta -1,4-glycanase Cex The catalytic domain from Cex (cex-cd) is in many ways a prototype for the retaining beta-1,4-glycanase enzymes, which are of fundamental importance in the cleavage of common beta -1,4-linkages in saccharides and of practical interest in the alternate energy source industry in treating common forms of biomass. In collaboration with Drs. Steve Withers, Tony Warren and colleagues at the University of British Columbia, we have been able to study the X-ray structures of cex-cd both alone and in complex with intermediates in the catalytic mechanism of the enzyme. This has led to new insights into the recognition by this protein of specific saccharide moeities. It also helped address the long-standing debate about the nature of the intermediate of this reaction: we provided strong evidence supporting the covalent intermediate model. We have also been able to identify specific contacts between the enzyme and the substrate that may assist in forming the tranition state of the reaction.