1gt9
From Proteopedia
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| - | [[Image:1gt9.jpg|left|200px]]<br /><applet load="1gt9" size=" | + | [[Image:1gt9.jpg|left|200px]]<br /><applet load="1gt9" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1gt9, resolution 1.38Å" /> | caption="1gt9, resolution 1.38Å" /> | ||
'''HIGH RESOLUTION CRYSTAL STRUCTURE OF A THERMOSTABLE SERINE-CARBOXYL TYPE PROTEINASE'''<br /> | '''HIGH RESOLUTION CRYSTAL STRUCTURE OF A THERMOSTABLE SERINE-CARBOXYL TYPE PROTEINASE'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1GT9 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]. Known structural/functional Site: <scene name='pdbsite=CA1:Ca Binding Site For Chain 2'>CA1</scene>. Full crystallographic information is available from [http:// | + | 1GT9 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]. Known structural/functional Site: <scene name='pdbsite=CA1:Ca+Binding+Site+For+Chain+2'>CA1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GT9 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: thermostable]] | [[Category: thermostable]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:42:27 2008'' |
Revision as of 07:42, 3 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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