2d1g
From Proteopedia
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| - | [[Image:2d1g.gif|left|200px]] | ||
| - | < | + | ==Structure of Francisella tularensis Acid Phosphatase A (AcpA) bound to orthovanadate== |
| - | + | <StructureSection load='2d1g' size='340' side='right'caption='[[2d1g]], [[Resolution|resolution]] 1.75Å' scene=''> | |
| - | You may | + | == Structural highlights == |
| - | + | <table><tr><td colspan='2'>[[2d1g]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Francisella_tularensis_subsp._novicida Francisella tularensis subsp. novicida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D1G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2D1G 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]] 1.75Å</td></tr> | |
| - | -- | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ETE:2-{2-[2-2-(METHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL'>ETE</scene>, <scene name='pdbligand=ETX:2-ETHOXYETHANOL'>ETX</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=VO4:VANADATE+ION'>VO4</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=2d1g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d1g OCA], [https://pdbe.org/2d1g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2d1g RCSB], [https://www.ebi.ac.uk/pdbsum/2d1g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2d1g ProSAT]</span></td></tr> | |
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0Q436_FRATN A0Q436_FRATN] | ||
| + | == 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/d1/2d1g_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=2d1g ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | AcpA is a respiratory burst-inhibiting acid phosphatase from the Centers for Disease Control and Prevention Category A bioterrorism agent Francisella tularensis and prototype of a superfamily of acid phosphatases and phospholipases C. We report the 1.75-A resolution crystal structure of AcpA complexed with the inhibitor orthovanadate, which is the first structure of any F. tularensis protein and the first for any member of this superfamily. The core domain is a twisted 8-stranded beta-sheet flanked by three alpha-helices on either side, with the active site located above the carboxyl-terminal edge of the beta-sheet. This architecture is unique among acid phosphatases and resembles that of alkaline phosphatase. Unexpectedly, the active site features a serine nucleophile and metal ion with octahedral coordination. Structure-based sequence analysis of the AcpA superfamily predicts that the hydroxyl nucleophile and metal center are also present in AcpA-like phospholipases C. These results imply a phospholipase C catalytic mechanism that is radically different from that of zinc metallophospholipases. | ||
| - | + | Structure of Francisella tularensis AcpA: prototype of a unique superfamily of acid phosphatases and phospholipases C.,Felts RL, Reilly TJ, Tanner JJ J Biol Chem. 2006 Oct 6;281(40):30289-98. Epub 2006 Aug 9. PMID:16899453<ref>PMID:16899453</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| + | <div class="pdbe-citations 2d1g" style="background-color:#fffaf0;"></div> | ||
| - | == | + | ==See Also== |
| - | + | *[[Acid phosphatase 3D structures|Acid phosphatase 3D structures]] | |
| - | [ | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Francisella tularensis subsp. novicida]] | [[Category: Francisella tularensis subsp. novicida]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Felts | + | [[Category: Felts RL]] |
| - | [[Category: Reilly | + | [[Category: Reilly TJ]] |
| - | [[Category: Tanner | + | [[Category: Tanner JJ]] |
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Current revision
Structure of Francisella tularensis Acid Phosphatase A (AcpA) bound to orthovanadate
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