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| A NOVEL VARIANT OF THE CATALYTIC TRIAD IN THE STREPTOMYCES-SCABIES ESTERASE |
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| Author(s): WEI YY, SCHOTTEL JL, DEREWENDA U, SWENSON L, PATKAR S, DEREWENDA ZS |
| Source: NATURE STRUCTURAL BIOLOGY Volume: 2 Issue: 3 Pages: 218-223 Published: MAR 1995 |
| Times Cited: 81 References: 43 |
| Abstract: The crystal structure of a novel esterase from Streptomyces scabies, a causal agent of the potato scab disease, was solved at 2.1 Angstrom resolution. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases. The active site contains a dyad of Ser 14 and His 283, closely resembling two of the three components of typical Ser-His-Asp(Glu) triads from other serine hydrolases, Proper orientation of the active site imidazol is maintained by a hydrogen bond between the N delta-H group and a main chain oxygen. Thus, the enzyme constitutes the first known natural variation of the chymotrypsin-like triad in which a carboxylic acid is replaced by a neutral hydrogen-bond acceptor. |
| Document Type: Article |
| Language: English |
Addresses:
1. UNIV ALBERTA, MED RES COUNCIL CANADA, DEPT BIOCHEM, PROT STRUCT & FUNCT GRP, EDMONTON, AB CANADA
2. UNIV MINNESOTA, DEPT BIOCHEM, ST PAUL, MN 55108 USA
3. NOVO NORDISK AS, RES LABS, COPENHAGEN, DENMARK |
| Publisher: NATURE PUBLISHING CO, 345 PARK AVE SOUTH, NEW YORK, NY 10010-1707 |
| Subject Category: Biochemistry & Molecular Biology; Biophysics; Cell Biology |
| IDS Number: RF666 |
| ISSN: 1072-8368 |
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| | | | | | | | | Record from Web of Science® | | | | | | | | | |