+
データを開く
-
基本情報
登録情報 | データベース: PDB / ID: 6mgt | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
タイトル | Crystal structure of alpha-Amino-beta-Carboxymuconate-epsilon-Semialdehyde Decarboxylase Mutant H110A | ||||||||||||
![]() | 2-amino-3-carboxymuconate 6-semialdehyde decarboxylase | ||||||||||||
![]() | LYASE / Holo structure / Decarboxylase | ||||||||||||
機能・相同性 | ![]() secondary metabolic process / : / : / carboxy-lyase activity / hydrolase activity / metal ion binding / cytosol 類似検索 - 分子機能 | ||||||||||||
生物種 | ![]() | ||||||||||||
手法 | ![]() ![]() ![]() | ||||||||||||
![]() | Yang, Y. / Daivs, I. / Matsui, T. / Rubalcava, I. / Liu, A. | ||||||||||||
資金援助 | ![]()
| ||||||||||||
![]() | ![]() タイトル: Quaternary structure of α-amino-β-carboxymuconate-ϵ-semialdehyde decarboxylase (ACMSD) controls its activity. 著者: Yu Yang / Ian Davis / Tsutomu Matsui / Ivan Rubalcava / Aimin Liu / ![]() 要旨: α-Amino-β-carboxymuconate-ϵ-semialdehyde decarboxylase (ACMSD) plays an important role in l-tryptophan degradation via the kynurenine pathway. ACMSD forms a homodimer and is functionally inactive ...α-Amino-β-carboxymuconate-ϵ-semialdehyde decarboxylase (ACMSD) plays an important role in l-tryptophan degradation via the kynurenine pathway. ACMSD forms a homodimer and is functionally inactive as a monomer because its catalytic assembly requires an arginine residue from a neighboring subunit. However, how the oligomeric state and self-association of ACMSD are controlled in solution remains unexplored. Here, we demonstrate that ACMSD from can self-assemble into homodimer, tetramer, and higher-order structures. Using size-exclusion chromatography coupled with small-angle X-ray scattering (SEC-SAXS) analysis, we investigated the ACMSD tetramer structure, and fitting the SAXS data with X-ray crystal structures of the monomeric component, we could generate a pseudo-atomic structure of the tetramer. This analysis revealed a tetramer model of ACMSD as a head-on dimer of dimers. We observed that the tetramer is catalytically more active than the dimer and is in equilibrium with the monomer and dimer. Substituting a critical residue of the dimer-dimer interface, His-110, altered the tetramer dissociation profile by increasing the higher-order oligomer portion in solution without changing the X-ray crystal structure. ACMSD self-association was affected by pH, ionic strength, and other electrostatic interactions. Alignment of ACMSD sequences revealed that His-110 is highly conserved in a few bacteria that utilize nitrobenzoic acid as a sole source of carbon and energy, suggesting a dedicated functional role of ACMSD's self-assembly into the tetrameric and higher-order structures. These results indicate that the dynamic oligomerization status potentially regulates ACMSD activity and that SEC-SAXS coupled with X-ray crystallography is a powerful tool for studying protein self-association. | ||||||||||||
履歴 |
|
-
構造の表示
構造ビューア | 分子: ![]() ![]() |
---|
-
ダウンロードとリンク
-
ダウンロード
PDBx/mmCIF形式 | ![]() | 142.8 KB | 表示 | ![]() |
---|---|---|---|---|
PDB形式 | ![]() | 110 KB | 表示 | ![]() |
PDBx/mmJSON形式 | ![]() | ツリー表示 | ![]() | |
その他 | ![]() |
-検証レポート
文書・要旨 | ![]() | 441.6 KB | 表示 | ![]() |
---|---|---|---|---|
文書・詳細版 | ![]() | 452 KB | 表示 | |
XML形式データ | ![]() | 24.8 KB | 表示 | |
CIF形式データ | ![]() | 33.4 KB | 表示 | |
アーカイブディレクトリ | ![]() ![]() | HTTPS FTP |
-関連構造データ
関連構造データ | ![]() 6mgsC ![]() 2hbvS S: 精密化の開始モデル C: 同じ文献を引用 ( |
---|---|
類似構造データ | |
その他のデータベース |
|
-
リンク
-
集合体
登録構造単位 | ![]()
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
単位格子 |
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
非結晶学的対称性 (NCS) | NCSドメイン:
NCSドメイン領域:
|