|1gt9, resolution 1.38Å ()|
HIGH RESOLUTION CRYSTAL STRUCTURE OF A THERMOSTABLE SERINE-CARBOXYL TYPE PROTEINASE, KUMAMOLISIN (KSCP)
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.
The 1.4 a crystal structure of kumamolysin: a thermostable serine-carboxyl-type proteinase., Comellas-Bigler M, Fuentes-Prior P, Maskos K, Huber R, Oyama H, Uchida K, Dunn BM, Oda K, Bode W, Structure. 2002 Jun;10(6):865-76. PMID:12057200
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
- Comellas-Bigler M, Fuentes-Prior P, Maskos K, Huber R, Oyama H, Uchida K, Dunn BM, Oda K, Bode W. The 1.4 a crystal structure of kumamolysin: a thermostable serine-carboxyl-type proteinase. Structure. 2002 Jun;10(6):865-76. PMID:12057200