1GT9

High resolution crystal structure of a thermostable serine-carboxyl type proteinase, kumamolisin (kscp)

1GT9 の概要

• エントリーDOI: 10.2210/pdb1gt9/pdb
• 関連するPDBエントリー: 1GTG
• 分子名称: KUMAMOLYSIN, CALCIUM ION, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: hydrolase, serine-carboxyl type proteinase, thermostable
• 由来する生物種: BACILLUS SUBTILIS
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 72906.31

構造登録者

Comellas-Bigler, M.,Fuentes-Prior, P.,Maskos, K.,Huber, R.,Oyama, H.,Uchida, K.,Dunn, B.M.,Oda, K.,Bode, W. (登録日: 2002-01-14, 公開日: 2002-06-13, 最終更新日: 2023-12-13)

主引用文献

Comellas-Bigler, M.,Fuentes-Prior, P.,Maskos, K.,Huber, R.,Oyama, H.,Uchida, K.,Dunn, B.M.,Oda, K.,Bode, W.
The 1.4 A Crystal Structure of Kumamolysin. A Thermostable Serine-Carboxyl-Type Proteinase
Structure, 10:865-, 2002

PubMed Abstract: Kumamolysin is a thermostable endopeptidase from Bacillus novosp. MN-32, exhibiting maximal proteolytic activity around pH 3. It belongs to the newly identified family of serine-carboxyl proteinases, which also includes CLN2, a human lysosomal homolog recently implicated in a fatal neurodegenerative disease. Kumamolysin and its complexes with two aldehyde inhibitors were crystallized, and their three-dimensional structures were solved and refined with X-ray data to 1.4 A resolution. As its Pseudomonas homolog, kumamolysin exhibits a Ser/Glu/Asp catalytic triad with particularly short interconnecting hydrogen bonds and an oxyanion hole enabling the reactive serine to attack substrate peptide bonds at quite acidic pH. An additional Glu/Trp pair, unique to kumamolysin, might further facilitate proton delocalization during nucleophilic attack, in particular at high temperature.

PubMed: 12057200
DOI: 10.1016/S0969-2126(02)00772-4

実験手法

X-RAY DIFFRACTION (1.38 Å)