7mpd: Difference between revisions
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<StructureSection load='7mpd' size='340' side='right'caption='[[7mpd]], [[Resolution|resolution]] 1.05Å' scene=''> | <StructureSection load='7mpd' size='340' side='right'caption='[[7mpd]], [[Resolution|resolution]] 1.05Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7mpd]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7MPD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7MPD FirstGlance]. <br> | <table><tr><td colspan='2'>[[7mpd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharolobus_solfataricus Saccharolobus solfataricus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7MPD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7MPD FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=ZLJ:2-chloroethane-1-sulfonic+acid'>ZLJ</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]] 1.05Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=ZLJ:2-chloroethane-1-sulfonic+acid'>ZLJ</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=7mpd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7mpd OCA], [https://pdbe.org/7mpd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7mpd RCSB], [https://www.ebi.ac.uk/pdbsum/7mpd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7mpd 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=7mpd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7mpd OCA], [https://pdbe.org/7mpd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7mpd RCSB], [https://www.ebi.ac.uk/pdbsum/7mpd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7mpd ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q97VZ7_SACS2 Q97VZ7_SACS2] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 7mpd" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 7mpd" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Tyrosine phosphatase 3D structures|Tyrosine phosphatase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Saccharolobus solfataricus]] | ||
[[Category: | [[Category: Hengge AC]] | ||
[[Category: | [[Category: Johnson SJ]] | ||
[[Category: | [[Category: Olsen KJ]] | ||
[[Category: | [[Category: Pinkston JA]] | ||
Latest revision as of 19:17, 18 October 2023
Structure of SsoPTP bound to 2-chloroethylsulfonateStructure of SsoPTP bound to 2-chloroethylsulfonate
Structural highlights
FunctionPublication Abstract from PubMedConformational dynamics are important factors in the function of enzymes, including protein tyrosine phosphatases (PTPs). Crystal structures of PTPs first revealed the motion of a protein loop bearing a conserved catalytic aspartic acid, and subsequent nuclear magnetic resonance and computational analyses have shown the presence of motions, involved in catalysis and allostery, within and beyond the active site. The tyrosine phosphatase from the thermophilic and acidophilic Sulfolobus solfataricus (SsoPTP) displays motions of its acid loop together with dynamics of its phosphoryl-binding P-loop and the Q-loop, the first instance of such motions in a PTP. All three loops share the same exchange rate, implying their motions are coupled. Further evidence of conformational flexibility comes from mutagenesis, kinetics, and isotope effect data showing that E40 can function as an alternate general acid to protonate the leaving group when the conserved acid, D69, is mutated to asparagine. SsoPTP is not the first PTP to exhibit an alternate general acid (after VHZ and TkPTP), but E40 does not correspond to the sequence or structural location of the alternate general acids in those precedents. A high-resolution X-ray structure with the transition state analogue vanadate clarifies the role of the active site arginine R102, which varied in structures of substrates bound to a catalytically inactive mutant. The coordinated motions of all three functional loops in SsoPTP, together with the function of an alternate general acid, suggest that catalytically competent conformations are present in solution that have not yet been observed in crystal structures. Significant Loop Motions in the SsoPTP Protein Tyrosine Phosphatase Allow for Dual General Acid Functionality.,Pinkston J, Jo J, Olsen KJ, Comer D, Glaittli CA, Loria JP, Johnson SJ, Hengge AC Biochemistry. 2021 Sep 8. doi: 10.1021/acs.biochem.1c00365. PMID:34496202[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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