2aut

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[[Image:2aut.png|left|200px]]
 
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==Crystal structure of Lys154Asn mutant of mature AphA of S. typhimurium==
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The line below this paragraph, containing "STRUCTURE_2aut", creates the "Structure Box" on the page.
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<StructureSection load='2aut' size='340' side='right'caption='[[2aut]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2aut]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium Salmonella enterica subsp. enterica serovar Typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AUT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AUT FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.25&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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{{STRUCTURE_2aut| PDB=2aut | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2aut FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2aut OCA], [https://pdbe.org/2aut PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2aut RCSB], [https://www.ebi.ac.uk/pdbsum/2aut PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2aut ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/APHA_SALTM APHA_SALTM] Dephosphorylates several organic phosphate monoesters. Also has a phosphotransferase activity catalyzing the transfer of low-energy phosphate groups from organic phosphate monoesters to free hydroxyl groups of various organic compounds (Probable).<ref>PMID:14501135</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/au/2aut_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=2aut ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The Salmonella typhimurium class B nonspecific acid phosphatase (AphA protein) belongs to the L2-haloacid dehalogenase superfamily. The conserved Lys-154 interacts with substrate phosphate, nucleophile Asp-46, and Asp-173 in the wild-type AphA protein. Asp-173 also interacts with Mg(II) water ligand and with main-chain amide of loop-4. We report here the mutational analysis of Lys-154 and Asp-173, the crystal structures of the K154N and K154R mutants, and the results of electrostatic potential calculations. The K154N, K154R and D173N mutants display significant reduction in the phosphatase activity. Lys-154 may not be responsible for a juxtaposition of the substrate phosphate and the aspartyl nucleophile, but has an hitherto unknown functional role of rendering the substrate phosphorous atom electron deficient. Nearly 10,000-fold increase in the K(d) value for dissociation of the cofactor Mg(II) observed for the D173N mutant correlates well with theoretically estimated change in the binding free energy of Mg(II).
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===Crystal structure of Lys154Asn mutant of mature AphA of S. typhimurium===
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Structural and mutational analyses reveal the functional role of active-site Lys-154 and Asp-173 of Salmonella typhimurium AphA protein.,Makde RD, Gupta GD, Mahajan SK, Kumar V Arch Biochem Biophys. 2007 Aug 1;464(1):70-9. Epub 2007 May 30. PMID:17570338<ref>PMID:17570338</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2aut" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_17570338}}, adds the Publication Abstract to the page
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*[[Acid phosphatase 3D structures|Acid phosphatase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 17570338 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_17570338}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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[[2aut]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_typhimurium Salmonella enterica subsp. enterica serovar typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AUT OCA].
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[[Category: Salmonella enterica subsp. enterica serovar Typhimurium]]
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[[Category: Gupta GD]]
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==Reference==
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[[Category: Kumar V]]
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<ref group="xtra">PMID:17570338</ref><ref group="xtra">PMID:14501135</ref><references group="xtra"/>
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[[Category: Makde RD]]
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[[Category: Acid phosphatase]]
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[[Category: Salmonella enterica subsp. enterica serovar typhimurium]]
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[[Category: Gupta, G D.]]
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[[Category: Kumar, V.]]
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[[Category: Makde, R D.]]
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[[Category: Class-b bacterial non-specific acid phosphatase]]
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[[Category: Hydrolase]]
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[[Category: Lys154asn mutant of mature apha]]
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[[Category: Metalloenzyme]]
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Current revision

Crystal structure of Lys154Asn mutant of mature AphA of S. typhimurium

PDB ID 2aut

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