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2enx
From Proteopedia
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| - | [[Image:2enx.jpg|left|200px]]<br /><applet load="2enx" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2enx, resolution 2.80Å" /> | ||
| - | '''Structure of the family II inorganic pyrophosphatase from Streptococcus agalactiae at 2.8 resolution'''<br /> | ||
| - | == | + | ==Structure of the family II inorganic pyrophosphatase from Streptococcus agalactiae at 2.8 resolution== |
| + | <StructureSection load='2enx' size='340' side='right'caption='[[2enx]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2enx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_agalactiae_A909 Streptococcus agalactiae A909]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ENX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ENX 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]] 2.8Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2PN:IMIDODIPHOSPHORIC+ACID'>2PN</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=TRP:TRYPTOPHAN'>TRP</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=2enx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2enx OCA], [https://pdbe.org/2enx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2enx RCSB], [https://www.ebi.ac.uk/pdbsum/2enx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2enx ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/PPAC_STRA1 PPAC_STRA1] | ||
| + | == 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/en/2enx_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=2enx ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
Streptococcus agalactiae, a prokaryote that causes infections in neonates and immunocompromised adults, has a serine/threonine protein kinase (STK) signalling cascade. The structure of one of the targets, a family II inorganic pyrophosphatase, has been solved by molecular replacement and refined at 2.80 A resolution to an R factor of 19.2% (R(free) = 26.7%). The two monomers in the asymmetric unit are related by a noncrystallographic twofold axis, but the biological dimer is formed by a crystallographic twofold. Each monomer contains the pyrophosphate analogue imidodiphosphate (PNP) and three metal ions per active site: two Mn(2+) ions in sites M1 and M2 and an Mg(2+) ion in site M3. The enzyme is in the closed conformation. Like other family II enzymes, the structure consists of two domains (residues 1-191 and 198-311), with the active site located between them. The conformation of Lys298 in the active site is different from those observed previously and it coordinates to the conserved DHH motif in a unique way. The structure suggests that Ser150, Ser194, Ser195 and Ser296 are the most likely targets for the Ser/Thr kinase and phosphatase because they are surface-accessible and either in the active site or in the hinge region between the two domains. | Streptococcus agalactiae, a prokaryote that causes infections in neonates and immunocompromised adults, has a serine/threonine protein kinase (STK) signalling cascade. The structure of one of the targets, a family II inorganic pyrophosphatase, has been solved by molecular replacement and refined at 2.80 A resolution to an R factor of 19.2% (R(free) = 26.7%). The two monomers in the asymmetric unit are related by a noncrystallographic twofold axis, but the biological dimer is formed by a crystallographic twofold. Each monomer contains the pyrophosphate analogue imidodiphosphate (PNP) and three metal ions per active site: two Mn(2+) ions in sites M1 and M2 and an Mg(2+) ion in site M3. The enzyme is in the closed conformation. Like other family II enzymes, the structure consists of two domains (residues 1-191 and 198-311), with the active site located between them. The conformation of Lys298 in the active site is different from those observed previously and it coordinates to the conserved DHH motif in a unique way. The structure suggests that Ser150, Ser194, Ser195 and Ser296 are the most likely targets for the Ser/Thr kinase and phosphatase because they are surface-accessible and either in the active site or in the hinge region between the two domains. | ||
| - | + | Structure of the Streptococcus agalactiae family II inorganic pyrophosphatase at 2.80 A resolution.,Rantanen MK, Lehtio L, Rajagopal L, Rubens CE, Goldman A Acta Crystallogr D Biol Crystallogr. 2007 Jun;63(Pt 6):738-43. Epub 2007, May 15. PMID:17505113<ref>PMID:17505113</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 2enx" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[Inorganic pyrophosphatase 3D structures|Inorganic pyrophosphatase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Streptococcus agalactiae A909]] | ||
| + | [[Category: Goldman A]] | ||
| + | [[Category: Lehtio L]] | ||
| + | [[Category: Rajagopal L]] | ||
| + | [[Category: Rantanen MK]] | ||
| + | [[Category: Rubens CE]] | ||
Current revision
Structure of the family II inorganic pyrophosphatase from Streptococcus agalactiae at 2.8 resolution
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