1UH9

Crystal structure of rhizopuspepsin at pH 7.0

1UH9 の概要

• エントリーDOI: 10.2210/pdb1uh9/pdb
• 関連するPDBエントリー: 1UH7 1UH8 2APR
• 分子名称: hizopuspepsin I (2 entities in total)
• 機能のキーワード: pepsin, aspartic proteinase, hydrolase
• 由来する生物種: Rhizopus microsporus var. chinensis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 34312.92

構造登録者

Prasad, B.V.L.S.,Suguna, K. (登録日: 2003-06-26, 公開日: 2004-06-26, 最終更新日: 2024-10-23)

主引用文献

Prasad, B.V.,Suguna, K.
Effect of pH on the structure of rhizopuspepsin.
Acta Crystallogr.,Sect.D, 59:1755-1761, 2003

PubMed Abstract: The crystal structure of rhizopuspepsin has been determined at three different pH values (4.6, 7.0 and 8.0) and compared with the previously reported structure at pH 6.0. A pH-sensitive region in the protein has been identified where certain structural changes take place at pH 8.0. An increase in the mobility of loops, weakening of hydrogen bonding and ionic interactions and a change in the water structure have been observed in this region. The loop between the first and the second beta-strands of the N-terminus shows increased mobility at high pH. This loop is known to be highly flexible in aspartic proteinases, aiding in relocating the N-terminal beta-strand segment in pH-related structural transformations. The observed changes in rhizopuspepsin indicate the triggering of a possible denatured state by high pH. The conformation of the active aspartates and the geometry of the catalytic site exhibit remarkable rigidity in this pH range.

PubMed: 14501114
DOI: 10.1107/S0907444903016068

実験手法

X-RAY DIFFRACTION (2 Å)