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| | <StructureSection load='6dt6' size='340' side='right'caption='[[6dt6]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='6dt6' size='340' side='right'caption='[[6dt6]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6dt6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_pestis"_(lehmann_and_neumann_1896)_migula_1900 "bacillus pestis" (lehmann and neumann 1896) migula 1900]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DT6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6DT6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6dt6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Yersinia_pestis Yersinia pestis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DT6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6DT6 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=VO4:VANADATE+ION'>VO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.101Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">yopH, YPCD1.67c ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=632 "Bacillus pestis" (Lehmann and Neumann 1896) Migula 1900])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=VO4:VANADATE+ION'>VO4</scene></td></tr> |
| - | <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=6dt6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dt6 OCA], [http://pdbe.org/6dt6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6dt6 RCSB], [http://www.ebi.ac.uk/pdbsum/6dt6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6dt6 ProSAT]</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=6dt6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dt6 OCA], [https://pdbe.org/6dt6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6dt6 RCSB], [https://www.ebi.ac.uk/pdbsum/6dt6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6dt6 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/O68720_YERPE O68720_YERPE] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Hengge, A C]] | + | [[Category: Yersinia pestis]] |
| - | [[Category: Johnson, S J]] | + | [[Category: Hengge AC]] |
| - | [[Category: Morales, Y]] | + | [[Category: Johnson SJ]] |
| - | [[Category: Hydrolase]] | + | [[Category: Morales Y]] |
| - | [[Category: Phosphatase]]
| + | |
| - | [[Category: Ptp]]
| + | |
| - | [[Category: Ptpase]]
| + | |
| - | [[Category: Yoph]]
| + | |
| Structural highlights
Function
O68720_YERPE
Publication Abstract from PubMed
To study factors that affect WPD-loop motion in protein tyrosine phosphatases (PTPs), a chimera of PTP1B and YopH was created by transposing the WPD loop from PTP1B to YopH. Several subsequent mutations proved to be necessary to obtain a soluble, active enzyme. That chimera, termed chimera 3, retains productive WPD-loop motions and general acid catalysis with a pH dependency similar to that of the native enzymes. Kinetic isotope effects show the mechanism and transition state for phosphoryl transfer are unaltered. Catalysis of the chimera is slower than that of either of its parent enzymes, although its rate is comparable to those of most native PTPs. X-ray crystallography and nuclear magnetic resonance were used to probe the structure and dynamics of chimera 3. The chimera's structure was found to sample an unproductive hyper-open conformation of its WPD loop, a geometry that has not been observed in either of the parents or in other native PTPs. The reduced catalytic rate is attributed to the protein's sampling of this conformation in solution, reducing the fraction in the catalytically productive loop-closed conformation.
A YopH PTP1B Chimera Shows the Importance of the WPD-Loop Sequence to the Activity, Structure, and Dynamics of Protein Tyrosine Phosphatases.,Moise G, Morales Y, Beaumont V, Caradonna T, Loria JP, Johnson SJ, Hengge AC Biochemistry. 2018 Aug 28. doi: 10.1021/acs.biochem.8b00663. PMID:30110154[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Moise G, Morales Y, Beaumont V, Caradonna T, Loria JP, Johnson SJ, Hengge AC. A YopH PTP1B Chimera Shows the Importance of the WPD-Loop Sequence to the Activity, Structure, and Dynamics of Protein Tyrosine Phosphatases. Biochemistry. 2018 Aug 28. doi: 10.1021/acs.biochem.8b00663. PMID:30110154 doi:http://dx.doi.org/10.1021/acs.biochem.8b00663
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