This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1t1e
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /><applet load="1t1e" size="450" color="white" frame="true" align="right" spinBox="true" caption="1t1e, resolution 1.18Å" /> '''High Resolution Crys...)
Next diff →
Revision as of 23:20, 24 November 2007
|
High Resolution Crystal Structure of the Intact Pro-Kumamolisin, a Sedolisin Type Proteinase (previously called Kumamolysin or KSCP)
Overview
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.
About this Structure
1T1E is a Single protein structure of sequence from Bacillus sp. mn-32 with CA as ligand. Full crystallographic information is available from OCA.
Reference
1.2 A crystal structure of the serine carboxyl proteinase pro-kumamolisin; structure of an intact pro-subtilase., Comellas-Bigler M, Maskos K, Huber R, Oyama H, Oda K, Bode W, Structure. 2004 Jul;12(7):1313-23. PMID:15242607
Page seeded by OCA on Sun Nov 25 01:28:06 2007
