Three-dimensional structure of the elastase of Pseudomonas aeruginosa at 1.5-A resolution.
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.
Thayer
M M
MM
Department of Chemistry and Biochemistry, University of Colorado, Boulder 80309.
Flaherty
K M
KM
McKay
D B
DB
D000595:Amino Acid Sequence; D002118:Calcium / Q000378:metabolism; D005583:Fourier Analysis; D008024:Ligands; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010196:Pancreatic Elastase / Q000737:chemistry*; D011550:Pseudomonas aeruginosa / Q000201:enzymology*; D016415:Sequence Alignment; D012689:Sequence Homology, Nucleic Acid; D013820:Thermolysin / Q000737:chemistry
D008024:Ligands; D010196:Pancreatic Elastase; D013820:Thermolysin; D002118:Calcium