Three-dimensional structure of the elastase of Pseudomonas aeruginosa at 1.5-A resolution.
Three-dimensional structure of the elastase of Pseudomonas aeruginosa at 1.5-A resolution.
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DOI：
10.2210/pdb1ezm/pdb
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发表时间：
1993-10
期刊：
影响因子：
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通讯作者：
M. M. Thayer-M.;K. Flaherty;D. Mckay
中科院分区：
文献类型：
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作者：
M. M. Thayer-M.;K. Flaherty;D. Mckay
铜绿假单胞菌弹性蛋白酶(PAE)是一种含301个氨基酸的锌金属蛋白酶。我们用1.5A分辨率的数据结晶和求解了PAE的三维结构，并将天然分子结构修正为R=0.188。PAE分子的总体三级结构与嗜热菌素的三级结构相似，其氨基酸序列同源性为28%。在这两种蛋白质中，几乎所有可能与底物相互作用的活性部位残基都是相同的。然而，在PAE中，活性部位裂解明显比在热裂解酶中更“开放”。
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.