1urr: Difference between revisions

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-[[Image:1urr.gif|left|200px]]<br />
-<applet load="1urr" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1urr, resolution 1.50&Aring;" />
-'''A NOVEL DROSOPHILA MELANOGASTER ACYLPHOSPHATASE (ACPDRO2)'''<br />
-==Overview==
+==A novel Drosophila Melanogaster Acylphosphatase (AcPDro2)==
-Analysis of the Drosophila melanogaster EST database led to the discovery, and cloning of a novel acylphosphatase. The CG18505 gene coding for a new, enzyme (AcPDro2) is clearly distinct from the previously described, CG16870Acyp gene, which also codes for a D. melanogaster acylphosphatase, (AcPDro). The putative catalytic residues, together with residues held to, stabilize the acylphosphatase fold, are conserved in the two encoded, proteins. Crystals of AcPDro2, which belong to the trigonal space group, P3(1)21, with unit-cell parameters a = b = 45.8, c = 98.6 angstroms, gamma, = 120 degrees, allowed the solution of the protein structure by molecular, replacement and its refinement to 1.5 angstroms resolution. The AcPDro2, active-site structure is discussed.
+<StructureSection load='1urr' size='340' side='right'caption='[[1urr]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1urr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1URR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1URR 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]] 1.5&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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=1urr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1urr OCA], [https://pdbe.org/1urr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1urr RCSB], [https://www.ebi.ac.uk/pdbsum/1urr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1urr ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/ACYP2_DROME ACYP2_DROME]
+== 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/ur/1urr_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1urr ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Analysis of the Drosophila melanogaster EST database led to the discovery and cloning of a novel acylphosphatase. The CG18505 gene coding for a new enzyme (AcPDro2) is clearly distinct from the previously described CG16870Acyp gene, which also codes for a D. melanogaster acylphosphatase (AcPDro). The putative catalytic residues, together with residues held to stabilize the acylphosphatase fold, are conserved in the two encoded proteins. Crystals of AcPDro2, which belong to the trigonal space group P3(1)21, with unit-cell parameters a = b = 45.8, c = 98.6 angstroms, gamma = 120 degrees, allowed the solution of the protein structure by molecular replacement and its refinement to 1.5 angstroms resolution. The AcPDro2 active-site structure is discussed.
-==About this Structure==
+Three-dimensional structural characterization of a novel Drosophila melanogaster acylphosphatase.,Zuccotti S, Rosano C, Ramazzotti M, Degl'Innocenti D, Stefani M, Manao G, Bolognesi M Acta Crystallogr D Biol Crystallogr. 2004 Jun;60(Pt 6):1177-9. Epub 2004, May 21. PMID:15159593<ref>PMID:15159593</ref>
-URR is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]] with GOL as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/Acylphosphatase Acylphosphatase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.7 3.6.1.7]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1URR OCA]].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-Three-dimensional structural characterization of a novel Drosophila melanogaster acylphosphatase., Zuccotti S, Rosano C, Ramazzotti M, Degl'Innocenti D, Stefani M, Manao G, Bolognesi M, Acta Crystallogr D Biol Crystallogr. 2004 Jun;60(Pt 6):1177-9. Epub 2004, May 21. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15159593 15159593]
+</div>
-[[Category: Acylphosphatase]]
+<div class="pdbe-citations 1urr" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Drosophila melanogaster]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Bolognesi, M.]]
+[[Category: Bolognesi M]]
-[[Category: Rosano, C.]]
+[[Category: Rosano C]]
-[[Category: Zuccotti, S.]]
+[[Category: Zuccotti S]]
-[[Category: GOL]]
-[[Category: acylphosphatase]]
-[[Category: enzyme]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 13:24:57 2007''