Download MendeleyThe 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, B.M., Oda, K., Bode, W.(2002) Structure 10: 865
- PubMed: 12057200
- DOI: https://doi.org/10.1016/s0969-2126(02)00772-4
- Primary Citation of Related Structures:
1GT9, 1GTG, 1GTJ, 1GTL - 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.
Organizational Affiliation:
Abteilung für Strukturforschung, Max-Planck-Institut für Biochemie, Am Klopferspitz 18 a, D82152, Planegg-Martinsried, Germany.
