3c7t: Difference between revisions
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New page: '''Unreleased structure''' The entry 3c7t is ON HOLD Authors: Chen, Y., Carpino, N., Nassar, N. Description: Crystal structure of the ecdysone phosphate phosphatase, EPPase, from Bombi... |
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==Crystal structure of the ecdysone phosphate phosphatase, EPPase, from Bombix mori in complex with tungstate== | |||
<StructureSection load='3c7t' size='340' side='right'caption='[[3c7t]], [[Resolution|resolution]] 1.76Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3c7t]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bombyx_mori Bombyx mori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C7T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3C7T 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]] 1.76Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=WO4:TUNGSTATE(VI)ION'>WO4</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=3c7t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c7t OCA], [https://pdbe.org/3c7t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3c7t RCSB], [https://www.ebi.ac.uk/pdbsum/3c7t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3c7t ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/EPP_BOMMO EPP_BOMMO] Steroid phosphatase which catalyzes the conversion of inactive phosphorylated ecdysteroids into their active forms (PubMed:12721294, PubMed:15738639, PubMed:18937503). Shows high activity towards ecdysone 22-phosphate (E22P) (PubMed:12721294). Has lower activity towards other ecdysteriod phosphates including 20-hydroxyecdysone 22-phosphate (20E22P) and 2-deoxyecdysone 22-phosphate (2dE22P) (PubMed:12721294). Also has protein tyrosine phosphatase activity (PubMed:18937503).<ref>PMID:12721294</ref> <ref>PMID:15738639</ref> <ref>PMID:18937503</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/c7/3c7t_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=3c7t ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Here, we present the crystal structure of the ecdysone phosphate phosphatase (EPPase) phosphoglycerate mutase (PGM) homology domain, the first structure of a steroid phosphate phosphatase. The structure reveals an alpha/beta-fold common to members of the two histidine (2H)-phosphatase superfamily with strong homology to the Suppressor of T-cell receptor signaling-1 (Sts-1 PGM) protein. The putative EPPase PGM active site contains signature residues shared by 2H-phosphatase enzymes, including a conserved histidine (His80) that acts as a nucleophile during catalysis. The physiological substrate ecdysone 22-phosphate was modeled in a hydrophobic cavity close to the phosphate-binding site. EPPase PGM shows limited substrate specificity with an ability to hydrolyze steroid phosphates, the phospho-tyrosine (pTyr) substrate analogue para-nitrophenylphosphate ( pNPP) and pTyr-containing peptides and proteins. Altogether, our data demonstrate a new protein tyrosine phosphatase (PTP) activity for EPPase. They suggest that EPPase and its closest homologues can be grouped into a distinct subfamily in the large 2H-phosphatase superfamily of proteins. | |||
Structural and functional characterization of the c-terminal domain of the ecdysteroid phosphate phosphatase from bombyx mori reveals a new enzymatic activity.,Chen Y, Jakoncic J, Wang J, Zheng X, Carpino N, Nassar N Biochemistry. 2008 Nov 18;47(46):12135-45. Epub 2008 Oct 21. PMID:18937503<ref>PMID:18937503</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3c7t" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bombyx mori]] | |||
[[Category: Large Structures]] | |||
[[Category: Carpino N]] | |||
[[Category: Chen Y]] | |||
[[Category: Nassar N]] | |||
