期刊
FEBS OPEN BIO
卷 6, 期 12, 页码 1170-1177出版社
WILEY
DOI: 10.1002/2211-5463.12132
关键词
antibiotic resistance; antibiotics; enzyme; enzyme structure; X-ray crystallography
资金
- Laboratory Directed Research and Development Program at Oak Ridge National Laboratory
- User Facilities Division, Office of Basic Energy Sciences, U.S. Department of Energy
- Office of Biological and Environmental Research at Oak Ridge National Laboratory's Center for Structural Molecular Biology (CSMB)
- Scientific User Facilities Division, Office of Basic Energy Sciences, U.S. Department of Energy
- U.S. Department of Energy, Office of Biological and Environmental Research [DE-AC02-06CH11357]
The role of the conserved residue Tyr105 in class A beta-lactamases has been the subject of investigation using both structural studies and saturation mutagenesis. Both have shown that while it does not need to be strictly conserved for activity, it is important for substrate recognition. With this in mind we determined the crystal structure of Toho1 beta-lactamase at 15 K to 1.10 angstrom resolution in complex with penicillin. As expected a ring-opened penicillin molecule bound to Ser70 the catalytic nucleophile, can clearly be seen in electron density in the active site. In addition to the trapped penicillin, however, are two additional intact ring-closed penicillin molecules, captured by the enzyme through noncovalent interactions at the edge of the active site.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据