1GTG

Crystal structure of the thermostable serine-carboxyl type proteinase, kumamolysin (kscp)

Summary for 1GTG

• Entry DOI: 10.2210/pdb1gtg/pdb
• Related: 1GT9 1GTJ 1GTL
• Descriptor: KUMAMOLYSIN, CALCIUM ION (3 entities in total)
• Functional Keywords: hydrolase, serine-carboxyl type proteinase, thermostable
• Biological source: BACILLUS NOVOSP. MN-32
• Total number of polymer chains: 1
• Total formula weight: 36357.09

Authors

Comellas-Bigler, M.,Fuentes-Prior, P.,Maskos, K.,Huber, R.,Oyama, H.,Uchida, K.,Dunn, B.M.,Oda, K.,Bode, W. (deposition date: 2002-01-15, release date: 2002-06-13, Last modification date: 2023-12-13)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.3 Å)