1SCJ

CRYSTAL STRUCTURE OF SUBTILISIN-PROPEPTIDE COMPLEX

Summary for 1SCJ

• Entry DOI: 10.2210/pdb1scj/pdb
• Descriptor: SUBTILISIN E, CALCIUM ION, ... (4 entities in total)
• Functional Keywords: hydrolase, subtilisin e - propeptide, serine protease
• Biological source: Bacillus subtilis; More
• Cellular location: Secreted: P04189 P04189
• Total number of polymer chains: 2
• Total formula weight: 35808.95

Authors

Berman, H.M.,Jain, S.C. (deposition date: 1998-04-29, release date: 1998-12-09, Last modification date: 2024-05-22)

Primary citation

Jain, S.C.,Shinde, U.,Li, Y.,Inouye, M.,Berman, H.M.
The crystal structure of an autoprocessed Ser221Cys-subtilisin E-propeptide complex at 2.0 A resolution.
J.Mol.Biol., 284:137-144, 1998

PubMed Abstract: We report here the crystallographic structure determination of an autoprocessed (Ser221Cys)-subtilisin E-propeptide complex at 2.0 A resolution. The subtilisin domain sequence has a single substitution (Ser221Cys) which has been shown to block the maturation process prior to degradation of the propeptide domain (77 residues) that acts as an intramolecular chaperon. This mutation, however, did not prevent the enzyme from cleaving its propeptide domain with a 60-80% efficiency. The current determination is the first example of a subtilisin E-propeptide complex which has been autoprocessed. A previous structure determination of a BPN'-prosegment complex has been reported in which the subtilisin domain was extensively mutated and a calcium binding loop was deleted. Further, in this earlier determination, the complex was formed by the addition of separately expressed propeptide domain. The structure determination reported here provides additional information about the nature of the interaction between the subtilisin and propeptide domains in this complex.

PubMed: 9811547
DOI: 10.1006/jmbi.1998.2161

Experimental method

X-RAY DIFFRACTION (2 Å)