1gt9

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{{STRUCTURE_1gt9| PDB=1gt9 | SCENE= }}
{{STRUCTURE_1gt9| PDB=1gt9 | SCENE= }}
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'''HIGH RESOLUTION CRYSTAL STRUCTURE OF A THERMOSTABLE SERINE-CARBOXYL TYPE PROTEINASE'''
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===HIGH RESOLUTION CRYSTAL STRUCTURE OF A THERMOSTABLE SERINE-CARBOXYL TYPE PROTEINASE===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_12057200}}
==About this Structure==
==About this Structure==
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[[Category: Serine-carboxyl type proteinase]]
[[Category: Serine-carboxyl type proteinase]]
[[Category: Thermostable]]
[[Category: Thermostable]]
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Revision as of 03:02, 1 July 2008

Image:1gt9.png

Template:STRUCTURE 1gt9

HIGH RESOLUTION CRYSTAL STRUCTURE OF A THERMOSTABLE SERINE-CARBOXYL TYPE PROTEINASE

Template:ABSTRACT PUBMED 12057200

About this Structure

1GT9 is a Single protein structure of sequence from Bacteria. 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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