1qvw: Difference between revisions

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New page: left|200px<br /><applet load="1qvw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qvw, resolution 1.9Å" /> '''Crystal structure of ...
 
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[[Image:1qvw.gif|left|200px]]<br /><applet load="1qvw" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1qvw.gif|left|200px]]<br /><applet load="1qvw" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1qvw, resolution 1.9&Aring;" />
caption="1qvw, resolution 1.9&Aring;" />
'''Crystal structure of the S. cerevisiae YDR533c protein'''<br />
'''Crystal structure of the S. cerevisiae YDR533c protein'''<br />


==Overview==
==Overview==
The ORF YDR533c from Saccharomyces cerevisiae codes for a 25.5 kDa protein, of unknown biochemical function. Transcriptome analysis of yeast has shown, that this gene is activated in response to various stress conditions, together with proteins belonging to the heat shock family. In order to, clarify its biochemical function, we determined the crystal structure of, YDR533c to 1.85 A resolution by the single anomalous diffraction method., The protein possesses an alpha/beta hydrolase fold and a putative, Cys-His-Glu catalytic triad common to a large enzyme family containing, proteases, amidotransferases, lipases, and esterases. The protein has, strong structural resemblance with the E. coli Hsp31 protein and the, intracellular protease I from Pyrococcus horikoshii, which are considered, class I and class III members of the Hsp31 family, respectively. Detailed, structural analysis strongly suggests that the YDR533c protein crystal, structure is the first one of a class II member of the Hsp31 family.
The ORF YDR533c from Saccharomyces cerevisiae codes for a 25.5 kDa protein of unknown biochemical function. Transcriptome analysis of yeast has shown that this gene is activated in response to various stress conditions together with proteins belonging to the heat shock family. In order to clarify its biochemical function, we determined the crystal structure of YDR533c to 1.85 A resolution by the single anomalous diffraction method. The protein possesses an alpha/beta hydrolase fold and a putative Cys-His-Glu catalytic triad common to a large enzyme family containing proteases, amidotransferases, lipases, and esterases. The protein has strong structural resemblance with the E. coli Hsp31 protein and the intracellular protease I from Pyrococcus horikoshii, which are considered class I and class III members of the Hsp31 family, respectively. Detailed structural analysis strongly suggests that the YDR533c protein crystal structure is the first one of a class II member of the Hsp31 family.


==About this Structure==
==About this Structure==
1QVW 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 GOL as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QVW OCA].  
1QVW 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=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QVW OCA].  


==Reference==
==Reference==
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[[Category: Leulliot, N.]]
[[Category: Leulliot, N.]]
[[Category: Quevillon-Cheruel, S.]]
[[Category: Quevillon-Cheruel, S.]]
[[Category: Tilbeurgh, H.van.]]
[[Category: Tilbeurgh, H van.]]
[[Category: GOL]]
[[Category: GOL]]
[[Category: alpha/beta hydrolase fold]]
[[Category: alpha/beta hydrolase fold]]
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[[Category: structural genomics]]
[[Category: structural genomics]]


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