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1txo

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==Crystal structure of the Mycobacterium tuberculosis serine/threonine phosphatase PstP/Ppp at 1.95 A.==
==Crystal structure of the Mycobacterium tuberculosis serine/threonine phosphatase PstP/Ppp at 1.95 A.==
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<StructureSection load='1txo' size='340' side='right' caption='[[1txo]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
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<StructureSection load='1txo' size='340' side='right'caption='[[1txo]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1txo]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TXO FirstGlance]. <br>
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<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>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
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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]] 1.95&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
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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=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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1txo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1txo OCA], [http://pdbe.org/1txo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1txo RCSB], [http://www.ebi.ac.uk/pdbsum/1txo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1txo ProSAT], [http://www.topsan.org/Proteins/TBSGC/1txo TOPSAN]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://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>
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[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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/tx/1txo_consurf.spt"</scriptWhenChecked>
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<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/initialview01.spt</scriptWhenUnchecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
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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=1txo ConSurf].
</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="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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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.
 
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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>
 
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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 1txo" style="background-color:#fffaf0;"></div>
 
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Phosphoprotein phosphatase]]
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[[Category: Large Structures]]
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[[Category: Alber, T]]
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[[Category: Mycobacterium tuberculosis]]
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[[Category: Good, M C]]
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[[Category: Alber T]]
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[[Category: Ng, H L]]
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[[Category: Good MC]]
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[[Category: Pullen, K E]]
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[[Category: Ng HL]]
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[[Category: Smith, S M]]
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[[Category: Pullen KE]]
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[[Category: Sung, P Y]]
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[[Category: Smith SM]]
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[[Category: Structural genomic]]
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[[Category: Sung PY]]
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[[Category: Hydrolase]]
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[[Category: PSI, Protein structure initiative]]
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[[Category: Pstp/ppp]]
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[[Category: Putative bacterial enzyme]]
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[[Category: Serine/threonine protein phosphatase]]
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[[Category: Tbsgc]]
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Current revision

Crystal structure of the Mycobacterium tuberculosis serine/threonine phosphatase PstP/Ppp at 1.95 A.

PDB ID 1txo

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