1txo: Difference between revisions

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OCA

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-[[Image:1txo.gif|left|200px]]<br /><applet load="1txo" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1txo, resolution 1.95&Aring;" />
-'''Crystal structure of the Mycobacterium tuberculosis serine/threonine phosphatase PstP/Ppp at 1.95 A.'''<br />
-==Overview==
+==Crystal structure of the Mycobacterium tuberculosis serine/threonine phosphatase PstP/Ppp at 1.95 A.==
-Serine/threonine protein phosphatases are central mediators of, phosphorylation-dependent signals in eukaryotes and a variety of, pathogenic bacteria. Here, we report the crystal structure of the, intracellular catalytic domain of Mycobacterium tuberculosis PstPpp, a, membrane-anchored phosphatase in the PP2C family. Despite sharing the fold, and two-metal center of human PP2Calpha, the PstPpp catalytic domain binds, a third Mn(2+) in a site created by a large shift in a previously, unrecognized flap subdomain adjacent to the active site. Mutations in this, site selectively increased the Michaelis constant for Mn(2+) in the, reaction of a noncognate, small-molecule substrate, p-nitrophenyl, phosphate. The PstP/Ppp structure reveals core functional motifs that, advance the framework for understanding the mechanisms of substrate, recognition, catalysis, and regulation of PP2C phosphatases.
+<StructureSection load='1txo' size='340' side='right'caption='[[1txo]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1txo]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TXO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TXO 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]] 1.95&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=1txo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1txo OCA], [https://pdbe.org/1txo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1txo RCSB], [https://www.ebi.ac.uk/pdbsum/1txo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1txo ProSAT], [https://www.topsan.org/Proteins/TBSGC/1txo TOPSAN]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/PSTP_MYCTU PSTP_MYCTU] The only predicted protein phosphatase in M.tuberculosis, it dephosphorylates at least 5 protein kinases (PknA, PknB, PknD, PknE and PknF) and the penicillin-binding protein PBPA.<ref>PMID:14575702</ref> <ref>PMID:12950916</ref> <ref>PMID:15967413</ref> <ref>PMID:16436437</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/tx/1txo_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=1txo ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Serine/threonine protein phosphatases are central mediators of phosphorylation-dependent signals in eukaryotes and a variety of pathogenic bacteria. Here, we report the crystal structure of the intracellular catalytic domain of Mycobacterium tuberculosis PstPpp, a membrane-anchored phosphatase in the PP2C family. Despite sharing the fold and two-metal center of human PP2Calpha, the PstPpp catalytic domain binds a third Mn(2+) in a site created by a large shift in a previously unrecognized flap subdomain adjacent to the active site. Mutations in this site selectively increased the Michaelis constant for Mn(2+) in the reaction of a noncognate, small-molecule substrate, p-nitrophenyl phosphate. The PstP/Ppp structure reveals core functional motifs that advance the framework for understanding the mechanisms of substrate recognition, catalysis, and regulation of PP2C phosphatases.
-==About this Structure==
+An alternate conformation and a third metal in PstP/Ppp, the M. tuberculosis PP2C-Family Ser/Thr protein phosphatase.,Pullen KE, Ng HL, Sung PY, Good MC, Smith SM, Alber T Structure. 2004 Nov;12(11):1947-54. PMID:15530359<ref>PMID:15530359</ref>
-TXO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis] with MN as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Phosphoprotein_phosphatase Phosphoprotein phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.16 3.1.3.16] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TXO OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-An alternate conformation and a third metal in PstP/Ppp, the M. tuberculosis PP2C-Family Ser/Thr protein phosphatase., Pullen KE, Ng HL, Sung PY, Good MC, Smith SM, Alber T, Structure. 2004 Nov;12(11):1947-54. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15530359 15530359]
+</div>
+<div class="pdbe-citations 1txo" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Mycobacterium tuberculosis]]
-[[Category: Phosphoprotein phosphatase]]
+[[Category: Alber T]]
-[[Category: Single protein]]
+[[Category: Good MC]]
-[[Category: Alber, T.]]
+[[Category: Ng HL]]
-[[Category: Good, M.C.]]
+[[Category: Pullen KE]]
-[[Category: Ng, H.L.]]
+[[Category: Smith SM]]
-[[Category: Pullen, K.E.]]
+[[Category: Sung PY]]
-[[Category: Smith, S.M.]]
-[[Category: Sung, P.Y.]]
-[[Category: TBSGC, TB.Structural.Genomics.Consortium.]]
-[[Category: MN]]
-[[Category: protein structure initiative]]
-[[Category: psi]]
-[[Category: pstp/ppp]]
-[[Category: putative bacterial enzyme]]
-[[Category: serine/threonine protein phosphatases]]
-[[Category: structural genomics]]
-[[Category: tb structural genomics consortium]]
-[[Category: tbsgc]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 02:55:54 2007''