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New page: left|200px<br /><applet load="1gcb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gcb, resolution 2.2Å" /> '''GAL6, YEAST BLEOMYCIN...
 
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[[Image:1gcb.jpg|left|200px]]<br /><applet load="1gcb" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1gcb.jpg|left|200px]]<br /><applet load="1gcb" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1gcb, resolution 2.2&Aring;" />
caption="1gcb, resolution 2.2&Aring;" />
'''GAL6, YEAST BLEOMYCIN HYDROLASE DNA-BINDING PROTEASE (THIOL)'''<br />
'''GAL6, YEAST BLEOMYCIN HYDROLASE DNA-BINDING PROTEASE (THIOL)'''<br />


==Overview==
==Overview==
Bleomycin hydrolase is a cysteine protease that hydrolyzes the anticancer, drug bleomycin. The homolog in yeast, Gal6, has recently been identified, and found to bind DNA and to act as a repressor in the Gal4 regulatory, system. The crystal structure of Gal6 at 2.2 A resolution reveals a, hexameric structure with a prominent central channel. The papain-like, active sites are situated within the central channel, in a manner, resembling the organization of active sites in the proteasome. The Gal6, channel is lined with 60 lysine residues from the six subunits, suggesting, a role in DNA binding. The carboxyl-terminal arm of Gal6 extends into the, active site cleft and may serve a regulatory function. Rather than each, residing in distinct, separable domains, the protease and DNA-binding, activities appear structurally intertwined in the hexamer, implying a, coupling of these two activities.
Bleomycin hydrolase is a cysteine protease that hydrolyzes the anticancer drug bleomycin. The homolog in yeast, Gal6, has recently been identified and found to bind DNA and to act as a repressor in the Gal4 regulatory system. The crystal structure of Gal6 at 2.2 A resolution reveals a hexameric structure with a prominent central channel. The papain-like active sites are situated within the central channel, in a manner resembling the organization of active sites in the proteasome. The Gal6 channel is lined with 60 lysine residues from the six subunits, suggesting a role in DNA binding. The carboxyl-terminal arm of Gal6 extends into the active site cleft and may serve a regulatory function. Rather than each residing in distinct, separable domains, the protease and DNA-binding activities appear structurally intertwined in the hexamer, implying a coupling of these two activities.


==About this Structure==
==About this Structure==
1GCB 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 SO4, HG and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GCB OCA].  
1GCB 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>, <scene name='pdbligand=HG:'>HG</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GCB OCA].  


==Reference==
==Reference==
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Johnston, S.A.]]
[[Category: Johnston, S A.]]
[[Category: Joshua-Tor, L.]]
[[Category: Joshua-Tor, L.]]
[[Category: Rees, D.C.]]
[[Category: Rees, D C.]]
[[Category: Xu, H.E.]]
[[Category: Xu, H E.]]
[[Category: GOL]]
[[Category: GOL]]
[[Category: HG]]
[[Category: HG]]
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[[Category: ring protein]]
[[Category: ring protein]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:56:06 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:48:36 2008''

Revision as of 10:48, 21 February 2008

File:1gcb.jpg


1gcb, resolution 2.2Å

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GAL6, YEAST BLEOMYCIN HYDROLASE DNA-BINDING PROTEASE (THIOL)

Overview

Bleomycin hydrolase is a cysteine protease that hydrolyzes the anticancer drug bleomycin. The homolog in yeast, Gal6, has recently been identified and found to bind DNA and to act as a repressor in the Gal4 regulatory system. The crystal structure of Gal6 at 2.2 A resolution reveals a hexameric structure with a prominent central channel. The papain-like active sites are situated within the central channel, in a manner resembling the organization of active sites in the proteasome. The Gal6 channel is lined with 60 lysine residues from the six subunits, suggesting a role in DNA binding. The carboxyl-terminal arm of Gal6 extends into the active site cleft and may serve a regulatory function. Rather than each residing in distinct, separable domains, the protease and DNA-binding activities appear structurally intertwined in the hexamer, implying a coupling of these two activities.

About this Structure

1GCB is a Single protein structure of sequence from Saccharomyces cerevisiae with SO4, HG and GOL as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of a conserved protease that binds DNA: the bleomycin hydrolase, Gal6., Joshua-Tor L, Xu HE, Johnston SA, Rees DC, Science. 1995 Aug 18;269(5226):945-50. PMID:7638617

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