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The X‐ray crystal structure of β‐ketoacyl [acyl carrier protein] synthase I
Author(s) -
Olsen Johan Gotthardt,
Kadziola Anders,
von Wettstein-Knowles Penny,
Siggaard-Andersen Mads,
Lindquist Ylva,
Larsen Sine
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)01303-4
Subject(s) - thiolase , acyl carrier protein , dimer , molecular replacement , crystal structure , active site , atp synthase , chemistry , stereochemistry , fatty acid synthase , binding site , hydrolase , substrate (aquarium) , enzyme , escherichia coli , crystallography , biochemistry , biology , organic chemistry , biosynthesis , ecology , gene , dehydrogenase
The crystal structure of the fatty acid elongating enzyme β‐ketoacyl [acyl carrier protein] synthase I (KAS I) from Escherichia coli has 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.