1t1g
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(New page: 200px<br /><applet load="1t1g" size="450" color="white" frame="true" align="right" spinBox="true" caption="1t1g, resolution 1.18Å" /> '''High Resolution Crys...)
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Revision as of 23:20, 24 November 2007
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High Resolution Crystal Structure of Mutant E23A of 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
1T1G is a Single protein structure of sequence from Bacillus sp. mn-32 with CA and SO4 as ligands. 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
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