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< | ==Crystal structure of yeast FSH1/YHR049W, a member of the serine hydrolase family== | ||
<StructureSection load='1ycd' size='340' side='right'caption='[[1ycd]], [[Resolution|resolution]] 1.70Å' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1ycd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YCD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YCD FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LI5:2-HYDROXY-4,5-DIOXOHEPTYL+HYDROGEN+PHOSPHONATE'>LI5</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ycd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ycd OCA], [https://pdbe.org/1ycd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ycd RCSB], [https://www.ebi.ac.uk/pdbsum/1ycd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ycd ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/FSH1_YEAST FSH1_YEAST] Serine hydrolase of unknown specificity.<ref>PMID:14645503</ref> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/yc/1ycd_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ycd ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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<ref>PMID:15802654</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1ycd" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | [[Category: Large Structures]] | ||
== | |||
< | |||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Coste | [[Category: Coste F]] | ||
[[Category: Graille | [[Category: Graille M]] | ||
[[Category: Janin | [[Category: Janin J]] | ||
[[Category: Leulliot | [[Category: Leulliot N]] | ||
[[Category: Quevillon-Cheruel | [[Category: Quevillon-Cheruel S]] | ||
[[Category: Tilbeurgh | [[Category: Van Tilbeurgh H]] | ||
Latest revision as of 10:41, 30 October 2024
Crystal structure of yeast FSH1/YHR049W, a member of the serine hydrolase familyCrystal structure of yeast FSH1/YHR049W, a member of the serine hydrolase family
Structural highlights
FunctionFSH1_YEAST Serine hydrolase of unknown specificity.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedYhr049w/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. 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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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