1t1e: Difference between revisions
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{{STRUCTURE_1t1e| PDB=1t1e | SCENE= }} | |||
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'''High Resolution Crystal Structure of the Intact Pro-Kumamolisin, a Sedolisin Type Proteinase (previously called Kumamolysin or KSCP)''' | '''High Resolution Crystal Structure of the Intact Pro-Kumamolisin, a Sedolisin Type Proteinase (previously called Kumamolysin or KSCP)''' | ||
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[[Category: Oda, K.]] | [[Category: Oda, K.]] | ||
[[Category: Oyama, H.]] | [[Category: Oyama, H.]] | ||
[[Category: | [[Category: Activation mechanism]] | ||
[[Category: | [[Category: Proenzyme]] | ||
[[Category: | [[Category: Prosubtilase]] | ||
[[Category: | [[Category: Sedolisin]] | ||
[[Category: | [[Category: Serine-carboxyl proteinase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:23:05 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 09:23, 3 May 2008
High Resolution Crystal Structure of the Intact Pro-Kumamolisin, a Sedolisin Type Proteinase (previously called Kumamolysin or KSCP)
OverviewOverview
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 StructureAbout this Structure
1T1E is a Single protein structure of sequence from Bacteria. Full crystallographic information is available from OCA.
ReferenceReference
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 Sat May 3 09:23:05 2008