1gt9
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Kumamolysin is a thermostable endopeptidase from Bacillus novosp. MN-32, exhibiting maximal proteolytic activity around pH 3. It belongs to the | + | Kumamolysin is a thermostable endopeptidase from Bacillus novosp. MN-32, exhibiting maximal proteolytic activity around pH 3. It belongs to the newly identified family of serine-carboxyl proteinases, which also includes CLN2, a human lysosomal homolog recently implicated in a fatal neurodegenerative disease. Kumamolysin and its complexes with two aldehyde inhibitors were crystallized, and their three-dimensional structures were solved and refined with X-ray data to 1.4 A resolution. As its Pseudomonas homolog, kumamolysin exhibits a Ser/Glu/Asp catalytic triad with particularly short interconnecting hydrogen bonds and an oxyanion hole enabling the reactive serine to attack substrate peptide bonds at quite acidic pH. An additional Glu/Trp pair, unique to kumamolysin, might further facilitate proton delocalization during nucleophilic attack, in particular at high temperature. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Bode, W.]] | [[Category: Bode, W.]] | ||
[[Category: Comellas-Bigler, M.]] | [[Category: Comellas-Bigler, M.]] | ||
| - | [[Category: Dunn, B | + | [[Category: Dunn, B M.]] |
[[Category: Fuentes-Prior, P.]] | [[Category: Fuentes-Prior, P.]] | ||
[[Category: Huber, R.]] | [[Category: Huber, R.]] | ||
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[[Category: thermostable]] | [[Category: thermostable]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:53:42 2008'' |
Revision as of 10:53, 21 February 2008
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HIGH RESOLUTION CRYSTAL STRUCTURE OF A THERMOSTABLE SERINE-CARBOXYL TYPE PROTEINASE
Overview
Kumamolysin is a thermostable endopeptidase from Bacillus novosp. MN-32, exhibiting maximal proteolytic activity around pH 3. It belongs to the newly identified family of serine-carboxyl proteinases, which also includes CLN2, a human lysosomal homolog recently implicated in a fatal neurodegenerative disease. Kumamolysin and its complexes with two aldehyde inhibitors were crystallized, and their three-dimensional structures were solved and refined with X-ray data to 1.4 A resolution. As its Pseudomonas homolog, kumamolysin exhibits a Ser/Glu/Asp catalytic triad with particularly short interconnecting hydrogen bonds and an oxyanion hole enabling the reactive serine to attack substrate peptide bonds at quite acidic pH. An additional Glu/Trp pair, unique to kumamolysin, might further facilitate proton delocalization during nucleophilic attack, in particular at high temperature.
About this Structure
1GT9 is a Single protein structure of sequence from Bacillus sp. mn-32 with and as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
The 1.4 a crystal structure of kumamolysin: a thermostable serine-carboxyl-type proteinase., Comellas-Bigler M, Fuentes-Prior P, Maskos K, Huber R, Oyama H, Uchida K, Dunn BM, Oda K, Bode W, Structure. 2002 Jun;10(6):865-76. PMID:12057200
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