| Autor: |
Olsen, Johan Gotthardt, Kadziola, Anders, von Wettstein-Knowles, Penny, Siggaard-Andersen, Mads, Lindquist, Ylva, Larsen, Sine |
| Zdroj: |
FEBS Letters; October 1999, Vol. 460 Issue: 1 p46-52, 7p |
| Abstrakt: |
The crystal structure of the fatty acid elongating enzyme β‐ketoacyl [acyl carrier protein] synthase I (KAS I) from Escherichia colihas been determined to 2.3 Å resolution by molecular replacement using the recently solved crystal structure of KAS II as a search model. The crystal contains two independent dimers in the asymmetric unit. KAS I assumes the thiolase αβαβα fold. Electrostatic potential distribution reveals an acyl carrier protein docking site and a presumed substrate binding pocket was detected extending the active site. Both subunits contribute to each substrate binding site in the dimer. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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