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Journal Article

The 1.4 angstrom crystal structure of kumamolysin: A thermostable serine-carboxyl-type proteinase

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http://pubman.mpdl.mpg.de/cone/persons/resource/persons77982

Fuentes-Prior,  P.
Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons78142

Huber,  R.
Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons77772

Bode,  W.
Fässler, Reinhard / Molecular Medicine, Max Planck Institute of Biochemistry, Max Planck Society;
Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society;
Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society;

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Citation

Comellas-Bigler, M., Fuentes-Prior, P., Maskos, K., Huber, R., Oyama, H., Uchida, K., et al. (2002). The 1.4 angstrom crystal structure of kumamolysin: A thermostable serine-carboxyl-type proteinase. Structure, 10(6), 865-876.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0010-6F14-B
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 Angstrom 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.