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spinqualitylabelsall models 1bs0, resolution 1.65Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

PLP-DEPENDENT ACYL-COA SYNTHASE

Overview

8-Amino-7-oxononanoate synthase (or 8-amino-7-ketopelargonate synthase; EC, 2.3.1.47; AONS) catalyses the decarboxylative condensation of l-alanine, and pimeloyl-CoA in the first committed step of biotin biosynthesis. We, have cloned, over-expressed and purified AONS from Escherichia coli and, determined the crystal structures of the apo and PLP-bound forms of the, enzyme. The protein is a symmetrical homodimer with a tertiary structure, and active site organisation similar to, but distinct from, those of other, PLP-dependent enzymes whose three-dimensional structures are known. The, critical PLP-binding lysine of AONS is located at the end of a deep cleft, that allows access of the pantothenate arm of pimeloyl-CoA. A cluster of, positively charged residues at the entrance to this cleft ... [(full description)]

About this Structure

1BS0 is a [Single protein] structure of sequence from [Escherichia coli] with SO4 as [ligand]. Active as [8-amino-7-oxononanoate synthase], with EC number [2.3.1.47]. Structure known Active Site: CAT. Full crystallographic information is available from [OCA].

Reference

The crystal structure of 8-amino-7-oxononanoate synthase: a bacterial PLP-dependent, acyl-CoA-condensing enzyme., Alexeev D, Alexeeva M, Baxter RL, Campopiano DJ, Webster SP, Sawyer L, J Mol Biol. 1998 Nov 27;284(2):401-19. PMID:9813126

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