1DD8: CRYSTAL STRUCTURE OF BETA-KETOACYL-[ACYL CARRIER PROTEIN] SYNTHASE I FROM ESCHERICHIA COLI

Citation:
Abstract
The crystal structure of the fatty acid elongating enzyme beta-ketoacyl [acyl carrier protein] synthase I (KAS I) from Escherichia coli has been determined to 2.3 A 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 alpha(beta)alpha(beta)alpha 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.
PDB ID: 1DD8Download
MMDB ID: 11543
PDB Deposition Date: 1999/11/9
Updated in MMDB: 1999/12
Experimental Method:
x-ray diffraction
Resolution: 2.3  Å
Source Organism:
Similar Structures:
Biological Unit for 1DD8: dimeric; determined by author and by software (PISA)
Molecular Components in 1DD8
Label Count Molecule
Proteins (2 molecules)
2
Beta-ketoacyl [acyl Carrier Protein] Synthase I(Gene symbol: fabB)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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