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1gtl

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[[Image:1gtl.gif|left|200px]]<br /><applet load="1gtl" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1gtl.gif|left|200px]]
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caption="1gtl, resolution 2.8&Aring;" />
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'''THE THERMOSTABLE SERINE-CARBOXYL TYPE PROTEINASE, KUMAMOLYSIN- COMPLEX WITH AC-ILE-PRO-PHE-CHO'''<br />
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{{Structure
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|PDB= 1gtl |SIZE=350|CAPTION= <scene name='initialview01'>1gtl</scene>, resolution 2.8&Aring;
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|SITE= <scene name='pdbsite=AC1:Ace+Binding+Site+For+Chain+4'>AC1</scene>
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=ACE:ACETYL GROUP'>ACE</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''THE THERMOSTABLE SERINE-CARBOXYL TYPE PROTEINASE, KUMAMOLYSIN- COMPLEX WITH AC-ILE-PRO-PHE-CHO'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1GTL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteria Bacteria] with <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=ACE:'>ACE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Ace+Binding+Site+For+Chain+4'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GTL OCA].
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1GTL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacteria Bacteria]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GTL OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12057200 12057200]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/12057200 12057200]
[[Category: Bacteria]]
[[Category: Bacteria]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: thermostable]]
[[Category: thermostable]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:53:49 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:27:45 2008''

Revision as of 09:27, 20 March 2008

Image:1gtl.gif


PDB ID 1gtl

Drag the structure with the mouse to rotate
, resolution 2.8Å
Sites:
Ligands: , and
Coordinates: save as pdb, mmCIF, xml



THE THERMOSTABLE SERINE-CARBOXYL TYPE PROTEINASE, KUMAMOLYSIN- COMPLEX WITH AC-ILE-PRO-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

1GTL 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

Page seeded by OCA on Thu Mar 20 11:27:45 2008

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