1T1E: High Resolution Crystal Structure Of The Intact Pro- Kumamolisin, A Sedolisin Type Proteinase (Previously Called Kumamolysin Or Kscp)

Kumamolisin, an extracellular proteinase derived from an acido/thermophilic Bacillus, belongs to the sedolisin family of endopeptidases characterized by a subtilisin-like fold and a Ser-Glu-Asp catalytic triad. In kumamolisin, the Asp82 carboxylate hydrogen bonds to Glu32-Trp129, which might act as a proton sink stabilizing the catalytic residues. The 1.2/1.3 A crystal structures of the Glu32-->Ala and Trp129-->Ala mutants show that both mutations affect the active-site conformation, causing a 95% activity decrease. In addition, the 1.2 A crystal structure of the Ser278-->Ala mutant of pro-kumamolisin was determined. The prodomain exhibits a half-beta sandwich core docking to the catalytic domain similarly as the equivalent subtilisin prodomains in their catalytic-domain complexes. This pro-kumamolisin structure displays, for the first time, the uncleaved linker segment running across the active site and connecting the prodomain with the properly folded catalytic domain. The structure strongly points to an initial intramolecular activation cleavage in subtilases, as presumed for pro-subtilisin and pro-furin.
PDB ID: 1T1EDownload
MMDB ID: 28623
PDB Deposition Date: 2004/4/16
Updated in MMDB: 2007/10
Experimental Method:
x-ray diffraction
Resolution: 1.18  Å
Source Organism:
Similar Structures:
Biological Unit for 1T1E: monomeric; determined by author
Molecular Components in 1T1E
Label Count Molecule
Protein (1 molecule)
Molecule annotation
Chemical (1 molecule)
* Click molecule labels to explore molecular sequence information.

Citing MMDB