1ycd: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
 
(12 intermediate revisions by the same user not shown)
Line 1: Line 1:
{{Seed}}
[[Image:1ycd.png|left|200px]]


<!--
==Crystal structure of yeast FSH1/YHR049W, a member of the serine hydrolase family==
The line below this paragraph, containing "STRUCTURE_1ycd", creates the "Structure Box" on the page.
<StructureSection load='1ycd' size='340' side='right'caption='[[1ycd]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<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>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</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>
{{STRUCTURE_1ycd|  PDB=1ycd  |  SCENE=  }}
<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 FSH1/YHR049W, a member of the serine hydrolase family===
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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
<!--
</div>
The line below this paragraph, {{ABSTRACT_PUBMED_15802654}}, adds the Publication Abstract to the page
<div class="pdbe-citations 1ycd" style="background-color:#fffaf0;"></div>
(as it appears on PubMed at http://www.pubmed.gov), where 15802654 is the PubMed ID number.
== References ==
-->
<references/>
{{ABSTRACT_PUBMED_15802654}}
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Large Structures]]
1YCD is a [[Single protein]] structure of sequence from [http://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].
 
==Reference==
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:[http://www.ncbi.nlm.nih.gov/pubmed/15802654 15802654]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Coste F]]
[[Category: Coste, F.]]
[[Category: Graille M]]
[[Category: Graille, M.]]
[[Category: Janin J]]
[[Category: Janin, J.]]
[[Category: Leulliot N]]
[[Category: Leulliot, N.]]
[[Category: Quevillon-Cheruel S]]
[[Category: Quevillon-Cheruel, S.]]
[[Category: Van Tilbeurgh H]]
[[Category: Tilbeurgh, H van.]]
[[Category: YSG, Paris-Sud Yeast Structural Genomics.]]
[[Category: Esterase]]
[[Category: Lipase]]
[[Category: Paris-sud yeast structural genomic]]
[[Category: S. cerevisiae]]
[[Category: Serine hydrolase]]
[[Category: Structural genomic]]
[[Category: Ysg]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 17:04:08 2008''

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

1ycd is a 2 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.7Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

FSH1_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 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[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Baxter SM, Rosenblum JS, Knutson S, Nelson MR, Montimurro JS, Di Gennaro JA, Speir JA, Burbaum JJ, Fetrow JS. Synergistic computational and experimental proteomics approaches for more accurate detection of active serine hydrolases in yeast. Mol Cell Proteomics. 2004 Mar;3(3):209-25. Epub 2003 Nov 25. PMID:14645503 doi:http://dx.doi.org/10.1074/mcp.M300082-MCP200
  2. Quevillon-Cheruel S, Leulliot N, Graille M, Hervouet N, Coste F, Benedetti H, Zelwer C, Janin J, Van Tilbeurgh H. Crystal structure of yeast YHR049W/FSH1, a member of the serine hydrolase family. Protein Sci. 2005 May;14(5):1350-6. Epub 2005 Mar 31. PMID:15802654 doi:10.1110/ps.051415905

1ycd, resolution 1.70Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA