1PQF

Glycine 24 to Serine mutation of aspartate decarboxylase

1PQF の概要

• エントリーDOI: 10.2210/pdb1pqf/pdb
• 関連するPDBエントリー: 1PPY 1PQE 1PQH 1PT0 1PT1 1PYQ 1PYU 1aw8
• 分子名称: Aspartate 1-decarboxylase, SULFATE ION (3 entities in total)
• 機能のキーワード: pyruvoyl-dependent decarboxylase, intramolecular protein self-processing, lyase
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cytoplasm: P0A790
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 31843.98

構造登録者

Schmitzberger, F.,Kilkenny, M.L.,Lobley, C.M.C.,Webb, M.E.,Vinkovic, M.,Matak-Vinkovic, D.,Witty, M.,Chirgadze, D.Y.,Smith, A.G.,Abell, C.,Blundell, T.L. (登録日: 2003-06-18, 公開日: 2003-11-18, 最終更新日: 2023-08-16)

主引用文献

Schmitzberger, F.,Kilkenny, M.L.,Lobley, C.M.C.,Webb, M.E.,Vinkovic, M.,Matak-Vinkovic, D.,Witty, M.,Chirgadze, D.Y.,Smith, A.G.,Abell, C.,Blundell, T.L.
Structural constraints on protein self-processing in L-aspartate-alpha-decarboxylase
Embo J., 22:6193-6204, 2003

PubMed Abstract: Aspartate decarboxylase, which is translated as a pro-protein, undergoes intramolecular self-cleavage at Gly24-Ser25. We have determined the crystal structures of an unprocessed native precursor, in addition to Ala24 insertion, Ala26 insertion and Gly24-->Ser, His11-->Ala, Ser25-->Ala, Ser25-->Cys and Ser25-->Thr mutants. Comparative analyses of the cleavage site reveal specific conformational constraints that govern self-processing and demonstrate that considerable rearrangement must occur. We suggest that Thr57 Ogamma and a water molecule form an 'oxyanion hole' that likely stabilizes the proposed oxyoxazolidine intermediate. Thr57 and this water molecule are probable catalytic residues able to support acid-base catalysis. The conformational freedom in the loop preceding the cleavage site appears to play a determining role in the reaction. The molecular mechanism of self-processing, presented here, emphasizes the importance of stabilization of the oxyoxazolidine intermediate. Comparison of the structural features shows significant similarity to those in other self-processing systems, and suggests that models of the cleavage site of such enzymes based on Ser-->Ala or Ser-->Thr mutants alone may lead to erroneous interpretations of the mechanism.

PubMed: 14633979
DOI: 10.1093/emboj/cdg575

実験手法

X-RAY DIFFRACTION (2 Å)