1W1Z

Structure of the plant like 5-Aminolaevulinic Acid Dehydratase from Chlorobium vibrioforme

1W1Z の概要

• エントリーDOI: 10.2210/pdb1w1z/pdb
• 分子名称: DELTA-AMINOLEVULINIC ACID DEHYDRATASE, LAEVULINIC ACID, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: synthase, tetrapyrrole biosynthesis, alad, porphyrin biosynthesis, heme biosynthesis, lyase, magnesium
• 由来する生物種: PROSTHECOCHLORIS VIBRIOFORMIS
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 73149.89

構造登録者

Coates, L.,Beaven, G.,Erskine, P.T.,Beale, S.I.,Avissar, Y.J.,Gill, R.,Mohammed, F.,Wood, S.P.,Shoolingin-Jordan, P.,Cooper, J.B. (登録日: 2004-06-24, 公開日: 2004-09-02, 最終更新日: 2024-11-13)

主引用文献

Coates, L.,Beaven, G.,Erskine, P.T.,Beale, S.I.,Avissar, Y.J.,Gill, R.,Mohammed, F.,Wood, S.P.,Shoolingin-Jordan, P.,Cooper, J.B.
The X-ray structure of the plant like 5-aminolaevulinic acid dehydratase from Chlorobium vibrioforme complexed with the inhibitor laevulinic acid at 2.6 A resolution.
J. Mol. Biol., 342:563-570, 2004

PubMed Abstract: 5-Aminolaevulinic acid dehydratase (ALAD), an early enzyme of the tetrapyrrole biosynthesis pathway, catalyses the dimerisation of 5-aminolaevulinic acid to form the pyrrole, porphobilinogen. ALAD from Chlorobium vibrioforme is shown to form a homo-octameric structure with 422 symmetry in which each subunit adopts a TIM-barrel fold with a 30 residue N-terminal arm extension. Pairs of monomers associate with their arms wrapped around each other. Four of these dimers interact principally via their arm regions to form octamers in which each active site is located on the surface. The active site contains two invariant lysine residues (200 and 253), one of which (Lys253) forms a Schiff base link with the bound substrate analogue, laevulinic acid. The carboxyl group of the laevulinic acid forms hydrogen bonds with the side-chains of Ser279 and Tyr318. The structure was examined to determine the location of the putative active-site magnesium ion, however, no evidence for the metal ion was found in the electron density map. This is in agreement with previous kinetic studies that have shown that magnesium stimulates but is not required for activity. A different site close to the active site flap, in which a putative magnesium ion is coordinated by a glutamate carboxyl and five solvent molecules may account for the stimulatory properties of magnesium ions on the enzyme.

PubMed: 15327955
DOI: 10.1016/j.jmb.2004.07.007

実験手法

X-RAY DIFFRACTION (2.6 Å)