1t1g
From Proteopedia
(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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| - | [[Image:1t1g.jpg|left|200px]]<br /><applet load="1t1g" size=" | + | [[Image:1t1g.jpg|left|200px]]<br /><applet load="1t1g" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1t1g, resolution 1.18Å" /> | caption="1t1g, resolution 1.18Å" /> | ||
'''High Resolution Crystal Structure of Mutant E23A of Kumamolisin, a sedolisin type proteinase (previously called Kumamolysin or KSCP)'''<br /> | '''High Resolution Crystal Structure of Mutant E23A of Kumamolisin, a sedolisin type proteinase (previously called Kumamolysin or KSCP)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Kumamolisin, an extracellular proteinase derived from an | + | 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== | ==About this Structure== | ||
| - | 1T1G is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_sp._mn-32 Bacillus sp. mn-32] with CA and SO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1T1G is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_sp._mn-32 Bacillus sp. mn-32] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T1G OCA]. |
==Reference== | ==Reference== | ||
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[[Category: subtilases]] | [[Category: subtilases]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:08:51 2008'' |
Revision as of 13:08, 21 February 2008
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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 and 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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