首页 | 本学科首页   官方微博 | 高级检索  
     


Three-dimensional structure of the elastase of Pseudomonas aeruginosa at 1.5-A resolution
Authors:M M Thayer  K M Flaherty  D B McKay
Affiliation:Department of Chemistry and Biochemistry, University of Colorado, Boulder 80309.
Abstract:Pseudomonas aeruginosa elastase (PAE) is a zinc metalloprotease with 301 amino acids. We have crystallized and solved the three-dimensional structure of PAE, using data to 1.5-A resolution, and have refined the native molecular structure to R = 0.188. The overall tertiary structure of the PAE molecule is similar to that of thermolysin, with which it shares 28% amino acid sequence identity. Nearly all of the active site residues that might potentially interact with substrates are identical in the two proteins. However, the active site cleft is significantly more "open" in PAE than in thermolysin.
Keywords:
设为首页 | 免责声明 | 关于勤云 | 加入收藏

Copyright©北京勤云科技发展有限公司  京ICP备09084417号