1EB3

YEAST 5-AMINOLAEVULINIC ACID DEHYDRATASE 4,7-DIOXOSEBACIC ACID COMPLEX

1EB3 の概要

• エントリーDOI: 10.2210/pdb1eb3/pdb
• 関連するPDBエントリー: 1AW5 1H7N 1H7O 1H7P 1H7R 1QML 1QNV 1YLV
• 分子名称: 5-AMINOLAEVULINIC ACID DEHYDRATASE, 4,7-DIOXOSEBACIC ACID, ZINC ION, ... (4 entities in total)
• 機能のキーワード: dehydratase, aldolase, tim barrel, tetrapyrrole synthesis
• 由来する生物種: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 37837.57

構造登録者

Erskine, P.T.,Coates, L.,Newbold, R.,Brindley, A.A.,Stauffer, F.,Wood, S.P.,Warren, M.J.,Cooper, J.B.,Shoolingin-Jordan, P.M.,Neier, R. (登録日: 2001-07-18, 公開日: 2001-08-02, 最終更新日: 2024-10-16)

主引用文献

Erskine, P.T.,Coates, L.,Newbold, R.,Brindley, A.A.,Stauffer, F.,Wood, S.P.,Warren, M.J.,Cooper, J.B.,Shoolingin-Jordan, P.M.,Neier, R.
The X-Ray Structure of Yeast 5-Aminolaevulinic Acid Dehydratase Complexed with Two Diacid Inhibitors
FEBS Lett., 503:196-, 2001

PubMed Abstract: The structures of 5-aminolaevulinic acid dehydratase complexed with two irreversible inhibitors (4-oxosebacic acid and 4,7-dioxosebacic acid) have been solved at high resolution. Both inhibitors bind by forming a Schiff base link with Lys 263 at the active site. Previous inhibitor binding studies have defined the interactions made by only one of the two substrate moieties (P-side substrate) which bind to the enzyme during catalysis. The structures reported here provide an improved definition of the interactions made by both of the substrate molecules (A- and P-side substrates). The most intriguing result is the novel finding that 4,7-dioxosebacic acid forms a second Schiff base with the enzyme involving Lys 210. It has been known for many years that P-side substrate forms a Schiff base (with Lys 263) but until now there has been no evidence that binding of A-side substrate involves formation of a Schiff base with the enzyme. A catalytic mechanism involving substrate linked to the enzyme through Schiff bases at both the A- and P-sites is proposed.

PubMed: 11513881
DOI: 10.1016/S0014-5793(01)02721-1

実験手法

X-RAY DIFFRACTION (1.75 Å)