1GE5

ZINC PEPTIDASE FROM GRIFOLA FRONDOSA

1GE5 の概要

• エントリーDOI: 10.2210/pdb1ge5/pdb
• 関連するPDBエントリー: 1G12 1GE6 1GE7
• 分子名称: PEPTIDYL-LYS METALLOENDOPEPTIDASE, alpha-D-mannopyranose, ZINC ION, ... (4 entities in total)
• 機能のキーワード: zinc coordinate, metalloprotease, hydrolase
• 由来する生物種: Grifola frondosa
• 細胞内の位置: Secreted : P81054
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 18303.99

構造登録者

Hori, T.,Kumasaka, T.,Yamamoto, M.,Nonaka, T.,Tanaka, N.,Hashimoto, Y.,Ueki, T.,Takio, K. (登録日: 2000-10-11, 公開日: 2001-03-14, 最終更新日: 2024-11-06)

主引用文献

Hori, T.,Kumasaka, T.,Yamamoto, M.,Nonaka, N.,Tanaka, N.,Hashimoto, Y.,Ueki, U.,Takio, K.
Structure of a new 'aspzincin' metalloendopeptidase from Grifola frondosa: implications for the catalytic mechanism and substrate specificity based on several different crystal forms.
Acta Crystallogr.,Sect.D, 57:361-368, 2001

PubMed Abstract: Crystal structures of a peptidyl-Lys metalloendopeptidase (MEP) from the edible mushroom Grifola frondosa (GfMEP) were solved in four crystal forms. This represents the first structure of the new family 'aspzincins' with a novel active-site architecture. The active site is composed of two helices and a loop region and includes the HExxH and GTxDxxYG motifs conserved among aspzincins. His117, His121 and Asp130 coordinate to the catalytic zinc ligands. An electrostatically negative region composed of Asp154 and Glu157 attracts a positively charged Lys side chain of a substrate in a specific manner. A Tyr133 side chain located on the S1' pocket had different configurations in two crystal forms and was not observed in the other crystal forms. The flexible Tyr133 plays two roles in the enzymatic function of GfMEP. The first is to provide a hydrophobic environment with Phe83 in order to accommodate the alkyl part of the Lys side chain of a substrate and the second is as a 'proton donor' to the oxyanion of the tetrahedral transition state to stabilize the reaction transition state.

PubMed: 11223512
DOI: 10.1107/S0907444900019740

実験手法

X-RAY DIFFRACTION (2 Å)