1PT1
Unprocessed Pyruvoyl Dependent Aspartate Decarboxylase with Histidine 11 Mutated to Alanine
1PT1 の概要
エントリーDOI | 10.2210/pdb1pt1/pdb |
関連するPDBエントリー | 1PPY 1PQE 1PQF 1PQH 1PT0 1PYQ 1PYU 1aw8 |
分子名称 | Aspartate 1-decarboxylase, SULFATE ION (3 entities in total) |
機能のキーワード | decarboxylase, pantothenate pathway, 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 | 31809.92 |
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: 2003-06-22, 公開日: 2003-11-11, 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 Cited by 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: 14633979DOI: 10.1093/emboj/cdg575 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.9 Å) |
構造検証レポート
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