1ycd: Difference between revisions

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New page: left|200px<br /><applet load="1ycd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ycd, resolution 1.70Å" /> '''Crystal structure of...
 
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[[Image:1ycd.gif|left|200px]]<br /><applet load="1ycd" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1ycd.gif|left|200px]]<br /><applet load="1ycd" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1ycd, resolution 1.70&Aring;" />
caption="1ycd, resolution 1.70&Aring;" />
'''Crystal structure of yeast FSH1/YHR049W, a member of the serine hydrolase family'''<br />
'''Crystal structure of yeast FSH1/YHR049W, a member of the serine hydrolase family'''<br />


==Overview==
==Overview==
Yhr049w/FSH1 was recently identified in a combined computational and, experimental proteomics analysis for the detection of active serine, hydrolases in yeast. This analysis suggested that FSH1 might be a, serine-type hydrolase belonging to the broad functional, alphabeta-hydrolase superfamily. In order to get insight into the, molecular function of this gene, it was targeted in our yeast structural, genomics project. The crystal structure of the protein confirms that it, contains a Ser/His/Asp catalytic triad that is part of a minimal, alpha/beta-hydrolase fold. The architecture of the putative active site, and analogies with other protein structures suggest that FSH1 may be an, esterase. This finding was further strengthened by the unexpected presence, of a compound covalently bound to the catalytic serine in the active site., Apparently, the enzyme was trapped with a reactive compound during the, purification process.
Yhr049w/FSH1 was recently identified in a combined computational and experimental proteomics analysis for the detection of active serine hydrolases in yeast. This analysis suggested that FSH1 might be a serine-type hydrolase belonging to the broad functional alphabeta-hydrolase superfamily. In order to get insight into the molecular function of this gene, it was targeted in our yeast structural genomics project. The crystal structure of the protein confirms that it contains a Ser/His/Asp catalytic triad that is part of a minimal alpha/beta-hydrolase fold. The architecture of the putative active site and analogies with other protein structures suggest that FSH1 may be an esterase. This finding was further strengthened by the unexpected presence of a compound covalently bound to the catalytic serine in the active site. Apparently, the enzyme was trapped with a reactive compound during the purification process.


==About this Structure==
==About this Structure==
1YCD 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 LI5 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1YCD OCA].  
1YCD 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=LI5:'>LI5</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YCD 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: YSG, Paris-Sud.Yeast.Structural.Genomics.]]
[[Category: YSG, Paris-Sud Yeast Structural Genomics.]]
[[Category: LI5]]
[[Category: LI5]]
[[Category: esterase]]
[[Category: esterase]]
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[[Category: ysg]]
[[Category: ysg]]


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Revision as of 17:03, 21 February 2008

File:1ycd.gif


1ycd, resolution 1.70Å

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Crystal structure of yeast FSH1/YHR049W, a member of the serine hydrolase family

OverviewOverview

Yhr049w/FSH1 was recently identified in a combined computational and experimental proteomics analysis for the detection of active serine hydrolases in yeast. This analysis suggested that FSH1 might be a serine-type hydrolase belonging to the broad functional alphabeta-hydrolase superfamily. In order to get insight into the molecular function of this gene, it was targeted in our yeast structural genomics project. The crystal structure of the protein confirms that it contains a Ser/His/Asp catalytic triad that is part of a minimal alpha/beta-hydrolase fold. The architecture of the putative active site and analogies with other protein structures suggest that FSH1 may be an esterase. This finding was further strengthened by the unexpected presence of a compound covalently bound to the catalytic serine in the active site. Apparently, the enzyme was trapped with a reactive compound during the purification process.

About this StructureAbout this Structure

1YCD is a Single protein structure of sequence from Saccharomyces cerevisiae with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of yeast YHR049W/FSH1, a member of the serine hydrolase family., Quevillon-Cheruel S, Leulliot N, Graille M, Hervouet N, Coste F, Benedetti H, Zelwer C, Janin J, Van Tilbeurgh H, Protein Sci. 2005 May;14(5):1350-6. Epub 2005 Mar 31. PMID:15802654

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