2cy7
From Proteopedia
(New page: 200px<br /> <applet load="2cy7" size="450" color="white" frame="true" align="right" spinBox="true" caption="2cy7, resolution 1.90Å" /> '''The crystal structu...) |
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| - | [[Image:2cy7.gif|left|200px]]<br /> | + | [[Image:2cy7.gif|left|200px]]<br /><applet load="2cy7" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2cy7" size=" | + | |
caption="2cy7, resolution 1.90Å" /> | caption="2cy7, resolution 1.90Å" /> | ||
'''The crystal structure of human Atg4B'''<br /> | '''The crystal structure of human Atg4B'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Reversible modification of Atg8 with phosphatidylethanolamine is crucial | + | Reversible modification of Atg8 with phosphatidylethanolamine is crucial for autophagy, the bulk degradation system conserved in eukaryotic cells. Atg4 is a novel cysteine protease that processes and deconjugates Atg8. Herein, we report the crystal structure of human Atg4B (HsAtg4B) at 1.9-A resolution. Despite no obvious sequence homology with known proteases, the structure of HsAtg4B shows a classical papain-like fold. In addition to the papain fold region, HsAtg4B has a small alpha/beta-fold domain. This domain is thought to be the binding site for Atg8 homologs. The active site cleft of HsAtg4B is masked by a loop (residues 259-262), implying a conformational change upon substrate binding. The structure and in vitro mutational analyses provide the basis for the specificity and catalysis of HsAtg4B. This will enable the design of Atg4-specific inhibitors that block autophagy. |
==About this Structure== | ==About this Structure== | ||
| - | 2CY7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 2CY7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CY7 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Ohsumi, Y.]] | [[Category: Ohsumi, Y.]] | ||
[[Category: Sugawara, K.]] | [[Category: Sugawara, K.]] | ||
| - | [[Category: Suzuki, N | + | [[Category: Suzuki, N N.]] |
[[Category: autophagy]] | [[Category: autophagy]] | ||
[[Category: papain-like fold]] | [[Category: papain-like fold]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:53:37 2008'' |
Revision as of 14:53, 21 February 2008
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The crystal structure of human Atg4B
Overview
Reversible modification of Atg8 with phosphatidylethanolamine is crucial for autophagy, the bulk degradation system conserved in eukaryotic cells. Atg4 is a novel cysteine protease that processes and deconjugates Atg8. Herein, we report the crystal structure of human Atg4B (HsAtg4B) at 1.9-A resolution. Despite no obvious sequence homology with known proteases, the structure of HsAtg4B shows a classical papain-like fold. In addition to the papain fold region, HsAtg4B has a small alpha/beta-fold domain. This domain is thought to be the binding site for Atg8 homologs. The active site cleft of HsAtg4B is masked by a loop (residues 259-262), implying a conformational change upon substrate binding. The structure and in vitro mutational analyses provide the basis for the specificity and catalysis of HsAtg4B. This will enable the design of Atg4-specific inhibitors that block autophagy.
About this Structure
2CY7 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural basis for the specificity and catalysis of human Atg4B responsible for mammalian autophagy., Sugawara K, Suzuki NN, Fujioka Y, Mizushima N, Ohsumi Y, Inagaki F, J Biol Chem. 2005 Dec 2;280(48):40058-65. Epub 2005 Sep 23. PMID:16183633
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