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| | ==Solution structure of a low molecular weight protein tyrosine phosphatase from Bacillus subtilis== | | ==Solution structure of a low molecular weight protein tyrosine phosphatase from Bacillus subtilis== |
| - | <StructureSection load='1zgg' size='340' side='right' caption='[[1zgg]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='1zgg' size='340' side='right'caption='[[1zgg]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1zgg]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_globigii"_migula_1900 "bacillus globigii" migula 1900]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZGG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ZGG FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1zgg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZGG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZGG FirstGlance]. <br> |
| - | </td></tr><tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] </span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1zgg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zgg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1zgg RCSB], [http://www.ebi.ac.uk/pdbsum/1zgg PDBsum]</span></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=1zgg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zgg OCA], [https://pdbe.org/1zgg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zgg RCSB], [https://www.ebi.ac.uk/pdbsum/1zgg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zgg ProSAT]</span></td></tr> |
| - | <table> | + | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/PAP_BACSU PAP_BACSU] Catalyzes the specific dephosphorylation of phosphoarginine residues in a large number of proteins. Counteracts the protein arginine kinase McsB in vivo. Can dephosphorylate CtsR-P; thus, can restore the DNA-binding ability of the CtsR repressor by reversing the McsB-mediated phosphorylation. Is the only active pArg phosphatase present in B.subtilis. Exhibits almost no activity against pSer, pThr, or pTyr peptides. Appears to play a role in B.subtilis stress resistance. Protein arginine phosphorylation has a physiologically important role and is involved in the regulation of many critical cellular processes, such as protein homeostasis, motility, competence, and stringent and stress responses, by regulating gene expression and protein activity.<ref>PMID:22517742</ref> <ref>PMID:23770242</ref> <ref>PMID:24263382</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> |
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zg/1zgg_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zg/1zgg_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> |
| | </jmolCheckbox> | | </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/chain_selection.php?pdb_ID=2ata 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=1zgg ConSurf]. |
| | <div style="clear:both"></div> | | <div style="clear:both"></div> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 1zgg" style="background-color:#fffaf0;"></div> |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus globigii migula 1900]] | + | [[Category: Bacillus subtilis]] |
| - | [[Category: Protein-tyrosine-phosphatase]] | + | [[Category: Large Structures]] |
| - | [[Category: Jin, C.]] | + | [[Category: Jin C]] |
| - | [[Category: Xia, B.]] | + | [[Category: Xia B]] |
| - | [[Category: Xu, H.]] | + | [[Category: Xu H]] |
| - | [[Category: Alpha/beta]]
| + | |
| - | [[Category: Four-stranded parallel beta sheet]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Structural genomic]]
| + | |
| Structural highlights
Function
PAP_BACSU Catalyzes the specific dephosphorylation of phosphoarginine residues in a large number of proteins. Counteracts the protein arginine kinase McsB in vivo. Can dephosphorylate CtsR-P; thus, can restore the DNA-binding ability of the CtsR repressor by reversing the McsB-mediated phosphorylation. Is the only active pArg phosphatase present in B.subtilis. Exhibits almost no activity against pSer, pThr, or pTyr peptides. Appears to play a role in B.subtilis stress resistance. Protein arginine phosphorylation has a physiologically important role and is involved in the regulation of many critical cellular processes, such as protein homeostasis, motility, competence, and stringent and stress responses, by regulating gene expression and protein activity.[1] [2] [3]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The low-molecular-weight (LMW) protein tyrosine phosphatases (PTPs) exist ubiquitously in prokaryotes and eukaryotes and play important roles in cellular processes. We report here the solution structure of YwlE, an LMW PTP identified from the gram-positive bacteria Bacillus subtilis. YwlE consists of a twisted central four-stranded parallel beta-sheet with seven alpha-helices packing on both sides. Similar to LMW PTPs from other organisms, the conformation of the YwlE active site is favorable for phosphotyrosine binding, indicating that it may share a common catalytic mechanism in the hydrolysis of phosphate on tyrosine residue in proteins. Though the overall structure resembles that of the eukaryotic LMW PTPs, significant differences were observed around the active site. Residue Asp115 is likely interacting with residue Arg13 through electrostatic interaction or hydrogen bond interaction to stabilize the conformation of the active cavity, which may be a unique character of bacterial LMW PTPs. Residues in the loop region from Phe40 to Thr48 forming a wall of the active cavity are more flexible than those in other regions. Ala41 and Gly45 are located near the active cavity and form a noncharged surface around it. These unique properties demonstrate that this loop may be involved in interaction with specific substrates. In addition, the results from spin relaxation experiments elucidate further insights into the mobility of the active site. The solution structure in combination with the backbone dynamics provides insights into the mechanism of substrate specificity of bacterial LMW PTPs.
Solution structure of a low-molecular-weight protein tyrosine phosphatase from Bacillus subtilis.,Xu H, Xia B, Jin C J Bacteriol. 2006 Feb;188(4):1509-17. PMID:16452434[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Elsholz AK, Turgay K, Michalik S, Hessling B, Gronau K, Oertel D, Mader U, Bernhardt J, Becher D, Hecker M, Gerth U. Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis. Proc Natl Acad Sci U S A. 2012 May 8;109(19):7451-6. doi:, 10.1073/pnas.1117483109. Epub 2012 Apr 19. PMID:22517742 doi:http://dx.doi.org/10.1073/pnas.1117483109
- ↑ Fuhrmann J, Mierzwa B, Trentini DB, Spiess S, Lehner A, Charpentier E, Clausen T. Structural basis for recognizing phosphoarginine and evolving residue-specific protein phosphatases in gram-positive bacteria. Cell Rep. 2013 Jun 27;3(6):1832-9. doi: 10.1016/j.celrep.2013.05.023. Epub 2013, Jun 13. PMID:23770242 doi:10.1016/j.celrep.2013.05.023
- ↑ Schmidt A, Trentini DB, Spiess S, Fuhrmann J, Ammerer G, Mechtler K, Clausen T. Quantitative phosphoproteomics reveals the role of protein arginine phosphorylation in the bacterial stress response. Mol Cell Proteomics. 2014 Feb;13(2):537-50. doi: 10.1074/mcp.M113.032292. Epub, 2013 Nov 20. PMID:24263382 doi:http://dx.doi.org/10.1074/mcp.M113.032292
- ↑ Xu H, Xia B, Jin C. Solution structure of a low-molecular-weight protein tyrosine phosphatase from Bacillus subtilis. J Bacteriol. 2006 Feb;188(4):1509-17. PMID:16452434 doi:188/4/1509
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