3TRS

The crystal structure of aspergilloglutamic peptidase from Aspergillus niger

3TRS の概要

• エントリーDOI: 10.2210/pdb3trs/pdb
• 分子名称: Aspergillopepsin-2 light chain, Aspergillopepsin-2 heavy chain, DIMETHYL SULFOXIDE, ... (4 entities in total)
• 機能のキーワード: aspergilloglutamic peptidase, glutamic peptidase, beta sandwich structure, hydrolase
• 由来する生物種: Aspergillus niger; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 44739.09

構造登録者

Sasaki, H.,Kubota, K.,Lee, W.C.,Ohtsuka, J.,Kojima, M.,Takahashi, K.,Tanokura, M. (登録日: 2011-09-10, 公開日: 2012-08-22, 最終更新日: 2024-11-20)

主引用文献

Sasaki, H.,Kubota, K.,Lee, W.C.,Ohtsuka, J.,Kojima, M.,Iwata, S.,Nakagawa, A.,Takahashi, K.,Tanokura, M.
The crystal structure of an intermediate dimer of aspergilloglutamic peptidase that mimics the enzyme-activation product complex produced upon autoproteolysis.
J.Biochem., 152:45-52, 2012

PubMed Abstract: Aspergilloglutamic peptidase from Aspergillus niger var. macrosporus (AGP) is one of the so-called pepstatin-insensitive acid endopeptidases, which are distinct from the well-studied aspartic peptidases. Among the known homologues of the glutamic peptidases, AGP is a unique two-chain enzyme with a light chain and a heavy chain bound non-covalently with each other, and thus is an interesting target for protein structure-function relationship studies. In this article, we report the crystal structure of a dimeric form of the enzyme at a resolution of 1.6 Å. This form has a unique structure in which the C-terminal region of the light chain of one of the molecules binds to the active site cleft of the other molecule like a part of a substrate. This form mimics the enzyme-activation product complex produced upon autoproteolysis, and provides a structural clue that could help to clarify the activation mechanism. This type of dimeric structure of a peptidase is here reported for the first time.

PubMed: 22569035
DOI: 10.1093/jb/mvs050

実験手法

X-RAY DIFFRACTION (1.6 Å)