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1gtj

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[[Image:1gtj.gif|left|200px]]<br />
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[[Image:1gtj.gif|left|200px]]<br /><applet load="1gtj" size="450" color="white" frame="true" align="right" spinBox="true"
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<applet load="1gtj" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1gtj, resolution 1.75&Aring;" />
caption="1gtj, resolution 1.75&Aring;" />
'''CRYSTAL STRUCTURE OF THE THERMOSTABLE SERINE-CARBOXYL TYPE PROTEINASE, KUMAMOLISIN (KSCP)- COMPLEX WITH AC-ILE-ALA-PHE-CHO'''<br />
'''CRYSTAL STRUCTURE OF THE THERMOSTABLE SERINE-CARBOXYL TYPE PROTEINASE, KUMAMOLISIN (KSCP)- COMPLEX WITH AC-ILE-ALA-PHE-CHO'''<br />
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==About this Structure==
==About this Structure==
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1GTJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteria Bacteria] with SO4, CA and ACE as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GTJ OCA].
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1GTJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteria Bacteria] with SO4, CA and ACE as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Ace Binding Site For Chain 2'>AC1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GTJ OCA].
==Reference==
==Reference==
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[[Category: thermostable]]
[[Category: thermostable]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 16:19:01 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 15:35:47 2007''

Revision as of 13:26, 18 December 2007


1gtj, resolution 1.75Å

Drag the structure with the mouse to rotate

CRYSTAL STRUCTURE OF THE THERMOSTABLE SERINE-CARBOXYL TYPE PROTEINASE, KUMAMOLISIN (KSCP)- COMPLEX WITH AC-ILE-ALA-PHE-CHO

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

1GTJ is a Single protein structure of sequence from Bacteria with SO4, CA and ACE 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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