2gi4: Difference between revisions

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-[[Image:2gi4.gif|left|200px]]
- {{Structure
+==Solution Structure of the Low Molecular Weight Protein Tyrosine Phosphatase from Campylobacter jejuni.==
-|PDB= 2gi4 |SIZE=350|CAPTION= <scene name='initialview01'>2gi4</scene>
+<StructureSection load='2gi4' size='340' side='right'caption='[[2gi4]]' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND=
+<table><tr><td colspan='2'>[[2gi4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Campylobacter_jejuni Campylobacter jejuni]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GI4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GI4 FirstGlance]. <br>
-|ACTIVITY= <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><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
-|GENE= CJ1258 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=197 Campylobacter jejuni])
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2gi4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gi4 OCA], [https://pdbe.org/2gi4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gi4 RCSB], [https://www.ebi.ac.uk/pdbsum/2gi4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gi4 ProSAT]</span></td></tr>
-|DOMAIN=
+</table>
-|RELATEDENTRY=
+== Function ==
-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2gi4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gi4 OCA], [http://www.ebi.ac.uk/pdbsum/2gi4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2gi4 RCSB]</span>
+[https://www.uniprot.org/uniprot/Q0P8Z8_CAMJE Q0P8Z8_CAMJE]
-}}
+== 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/gi/2gi4_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=2gi4 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+A putative low molecular weight protein tyrosine phosphatase (LMW-PTP) was identified in the genome sequence of the bacterial pathogen, Campylobacter jejuni. This novel gene, cj1258, has sequence homology with a distinctive class of phosphatases widely distributed among prokaryotes and eukaryotes. We report here the solution structure of Cj1258 established by high-resolution NMR spectroscopy using NOE-derived distance restraints, hydrogen bond data, and torsion angle restraints. The three-dimensional structure consists of a central four-stranded parallel beta-sheet flanked by five alpha-helices, revealing an overall structural topology similar to those of the eukaryotic LMW-PTPs, such as human HCPTP-A, bovine BPTP, and Saccharomyces cerevisiae LTP1, and to those of the bacterial LMW-PTPs MPtpA from Mycobacterium tuberculosis and YwlE from Bacillus subtilis. The active site of the enzyme is flexible in solution and readily adapts to the binding of ligands, such as the phosphate ion. An NMR-based screen was carried out against a number of potential inhibitors and activators, including phosphonomethylphenylalanine, derivatives of the cinnamic acid, 2-hydroxy-5-nitrobenzaldehyde, cinnamaldehyde, adenine, and hypoxanthine. Despite its bacterial origin, both the three-dimensional structure and ligand-binding properties of Cj1258 suggest that this novel phosphatase may have functional roles close to those of eukaryotic and mammalian tyrosine phosphatases. The three-dimensional structure along with mapping of small-molecule binding will be discussed in the context of developing high-affinity inhibitors of this novel LMW-PTP.
-'''Solution Structure of the Low Molecular Weight Protein Tyrosine Phosphatase from Campylobacter jejuni.'''
+Three-dimensional structure and ligand interactions of the low molecular weight protein tyrosine phosphatase from Campylobacter jejuni.,Tolkatchev D, Shaykhutdinov R, Xu P, Plamondon J, Watson DC, Young NM, Ni F Protein Sci. 2006 Oct;15(10):2381-94. PMID:17008719<ref>PMID:17008719</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2gi4" style="background-color:#fffaf0;"></div>
-==Overview==
+==See Also==
-A putative low molecular weight protein tyrosine phosphatase (LMW-PTP) was identified in the genome sequence of the bacterial pathogen, Campylobacter jejuni. This novel gene, cj1258, has sequence homology with a distinctive class of phosphatases widely distributed among prokaryotes and eukaryotes. We report here the solution structure of Cj1258 established by high-resolution NMR spectroscopy using NOE-derived distance restraints, hydrogen bond data, and torsion angle restraints. The three-dimensional structure consists of a central four-stranded parallel beta-sheet flanked by five alpha-helices, revealing an overall structural topology similar to those of the eukaryotic LMW-PTPs, such as human HCPTP-A, bovine BPTP, and Saccharomyces cerevisiae LTP1, and to those of the bacterial LMW-PTPs MPtpA from Mycobacterium tuberculosis and YwlE from Bacillus subtilis. The active site of the enzyme is flexible in solution and readily adapts to the binding of ligands, such as the phosphate ion. An NMR-based screen was carried out against a number of potential inhibitors and activators, including phosphonomethylphenylalanine, derivatives of the cinnamic acid, 2-hydroxy-5-nitrobenzaldehyde, cinnamaldehyde, adenine, and hypoxanthine. Despite its bacterial origin, both the three-dimensional structure and ligand-binding properties of Cj1258 suggest that this novel phosphatase may have functional roles close to those of eukaryotic and mammalian tyrosine phosphatases. The three-dimensional structure along with mapping of small-molecule binding will be discussed in the context of developing high-affinity inhibitors of this novel LMW-PTP.
+*[[Tyrosine phosphatase 3D structures|Tyrosine phosphatase 3D structures]]
+== References ==
-==About this Structure==
+<references/>
-GI4 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Campylobacter_jejuni Campylobacter jejuni]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GI4 OCA].
+__TOC__
+</StructureSection>
-==Reference==
-Three-dimensional structure and ligand interactions of the low molecular weight protein tyrosine phosphatase from Campylobacter jejuni., Tolkatchev D, Shaykhutdinov R, Xu P, Plamondon J, Watson DC, Young NM, Ni F, Protein Sci. 2006 Oct;15(10):2381-94. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17008719 17008719]
 [[Category: Campylobacter jejuni]]
-[[Category: Protein-tyrosine-phosphatase]]
+[[Category: Large Structures]]
-[[Category: Single protein]]
+[[Category: Ni F]]
-[[Category: Ni, F.]]
+[[Category: Shaykhutdinov R]]
-[[Category: Shaykhutdinov, R.]]
+[[Category: Tolkatchev D]]
-[[Category: Tolkatchev, D.]]
+[[Category: Xu P]]
-[[Category: Xu, P.]]
-[[Category: bacterial phosphatase]]
-[[Category: hydrolase]]
-[[Category: low molecular weight]]
-[[Category: phosphatase]]
-[[Category: prokaryotic phosphatase]]
-[[Category: protein tyrosine phosphatase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:16:57 2008''