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3gcb

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[[Image:3gcb.gif|left|200px]]<br /><applet load="3gcb" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:3gcb.gif|left|200px]]
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caption="3gcb, resolution 1.87&Aring;" />
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'''GAL6 (YEAST BLEOMYCIN HYDROLASE) MUTANT C73A/DELTAK454'''<br />
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{{Structure
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|PDB= 3gcb |SIZE=350|CAPTION= <scene name='initialview01'>3gcb</scene>, resolution 1.87&Aring;
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|SITE= <scene name='pdbsite=A73:Nucleophilic+CYS+Mutated+To+ALA'>A73</scene> and <scene name='pdbsite=NUL:Catalytic+Residues'>NUL</scene>
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
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|ACTIVITY=
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|GENE= GAL6C73ADELK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
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}}
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'''GAL6 (YEAST BLEOMYCIN HYDROLASE) MUTANT C73A/DELTAK454'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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3GCB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Sites: <scene name='pdbsite=A73:Nucleophilic+CYS+Mutated+To+ALA'>A73</scene> and <scene name='pdbsite=NUL:Catalytic+Residues'>NUL</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GCB OCA].
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3GCB is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GCB OCA].
==Reference==
==Reference==
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The unusual active site of Gal6/bleomycin hydrolase can act as a carboxypeptidase, aminopeptidase, and peptide ligase., Zheng W, Johnston SA, Joshua-Tor L, Cell. 1998 Apr 3;93(1):103-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9546396 9546396]
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The unusual active site of Gal6/bleomycin hydrolase can act as a carboxypeptidase, aminopeptidase, and peptide ligase., Zheng W, Johnston SA, Joshua-Tor L, Cell. 1998 Apr 3;93(1):103-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9546396 9546396]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: self-compartmentalizing protease]]
[[Category: self-compartmentalizing protease]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:09:28 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 19:04:56 2008''

Revision as of 17:04, 20 March 2008


PDB ID 3gcb

Drag the structure with the mouse to rotate
, resolution 1.87Å
Sites: and
Ligands: and
Gene: GAL6C73ADELK (Saccharomyces cerevisiae)
Coordinates: save as pdb, mmCIF, xml



GAL6 (YEAST BLEOMYCIN HYDROLASE) MUTANT C73A/DELTAK454


Overview

The Gal6 protease is in a class of cysteine peptidases identified by their ability to inactivate the anti-cancer drug bleomycin. The protein forms a barrel structure with the active sites embedded in a channel as in the proteasome. In Gal6 the C termini lie in the active site clefts. We show that Gal6 acts as a carboxypeptidase on its C terminus to convert itself to an aminopeptidase and peptide ligase. The substrate specificity of the peptidase activity is determined by the position of the C terminus of Gal6 rather than the sequence of the substrate. We propose a model to explain these diverse activities and Gal6's singular ability to inactivate bleomycin.

About this Structure

3GCB is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

The unusual active site of Gal6/bleomycin hydrolase can act as a carboxypeptidase, aminopeptidase, and peptide ligase., Zheng W, Johnston SA, Joshua-Tor L, Cell. 1998 Apr 3;93(1):103-9. PMID:9546396

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