1ESA
DIRECT STRUCTURE OBSERVATION OF AN ACYL-ENZYME INTERMEDIATE IN THE HYDROLYSIS OF AN ESTER SUBSTRATE BY ELASTASE
Summary for 1ESA
| Entry DOI | 10.2210/pdb1esa/pdb |
| Descriptor | PORCINE PANCREATIC ELASTASE, CALCIUM ION, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | hydrolase(serine proteinase) |
| Biological source | Sus scrofa (pig) |
| Cellular location | Secreted: P00772 |
| Total number of polymer chains | 1 |
| Total formula weight | 26160.24 |
| Authors | Ding, X.,Rasmussen, B.,Petsko, G.A.,Ringe, D. (deposition date: 1994-02-04, release date: 1994-04-30, Last modification date: 2024-10-30) |
| Primary citation | Ding, X.,Rasmussen, B.F.,Petsko, G.A.,Ringe, D. Direct structural observation of an acyl-enzyme intermediate in the hydrolysis of an ester substrate by elastase. Biochemistry, 33:9285-9293, 1994 Cited by PubMed Abstract: The method of X-ray crystallographic cryoenzymology has been used to determine the crystal structure of a kinetically significant species on the reaction pathway of a crystalline enzyme. The structure of a specific acyl-enzyme intermediate in the elastase-catalyzed hydrolysis of the N-carbobenzoxy-L-alanine p-nitrophenyl ester has been determined and refined against X-ray diffraction data at 2.3-A resolution. The difference Fourier electron density map clearly shows electron density for the trapped acyl-enzyme. The acyl-enzyme was formed at -26 degrees C and was stabilized at -55 degrees C during data collection, taking advantage of the glass transition in protein dynamics that occurs at around -50 degrees C. PubMed: 8049229DOI: 10.1021/bi00197a032 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.65 Å) |
Structure validation
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