1BS0

PLP-DEPENDENT ACYL-COA SYNTHASE

1BS0 の概要

• エントリーDOI: 10.2210/pdb1bs0/pdb
• 分子名称: PROTEIN (8-AMINO-7-OXONANOATE SYNTHASE), SULFATE ION (3 entities in total)
• 機能のキーワード: plp-dependent acyl-coa synthase, biotin biosynthesis, 8-amino-7-oxonanoate synthase, 8-amino-7-ketopelargonate synthase, transferase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 41929.36

構造登録者

Alexeev, D.,Alexeeva, M.,Baxter, R.L.,Campopiano, D.J.,Webster, S.P.,Sawyer, L. (登録日: 1998-08-31, 公開日: 1999-08-27, 最終更新日: 2023-12-27)

主引用文献

Alexeev, D.,Alexeeva, M.,Baxter, R.L.,Campopiano, D.J.,Webster, S.P.,Sawyer, L.
The crystal structure of 8-amino-7-oxononanoate synthase: a bacterial PLP-dependent, acyl-CoA-condensing enzyme.
J.Mol.Biol., 284:401-419, 1998

PubMed Abstract: 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 forms a putative diphosphate binding site for CoA. The structure of E. coli AONS enables identification of the key residues of the PLP-binding site and thus provides a framework with which to understand the biochemical mechanism, which is similar to that catalysed by 5-aminolevulinate synthase and two other alpha-oxoamine synthases. Although AONS has a low overall sequence similarity with the catalytic domains of other alpha-oxoamine synthases, the structure reveals the regions of significant identity to be functionally important. This suggests that the organisation of the conserved catalytic residues in the active site is similar for all enzymes of this sub-class of PLP-dependent enzymes and they share a common mechanism. Knowledge of the three-dimensional structure of AONS will enable characterisation of the structural features of this enzyme sub-family that are responsible for this important type of reaction.

PubMed: 9813126
DOI: 10.1006/jmbi.1998.2086

実験手法

X-RAY DIFFRACTION (1.65 Å)