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TitleSignificant Loop Motions in the SsoPTP Protein Tyrosine Phosphatase Allow for Dual General Acid Functionality.
Journal, issue, pagesBiochemistry, Vol. 60, Page 2888-2901, Year 2021
Publish dateMay 4, 2021 (structure data deposition date)
AuthorsPinkston, J. / Jo, J. / Olsen, K.J. / Comer, D. / Glaittli, C.A. / Loria, J.P. / Johnson, S.J. / Hengge, A.C.
External linksBiochemistry / PubMed:34496202
MethodsX-ray diffraction
Resolution1.05 - 1.75 Å
Structure data

PDB-7mpc:
Structure of SsoPTP bound to vanadate
Method: X-RAY DIFFRACTION / Resolution: 1.75 Å

PDB-7mpd:
Structure of SsoPTP bound to 2-chloroethylsulfonate
Method: X-RAY DIFFRACTION / Resolution: 1.05 Å

Chemicals

ChemComp-VO4:
VANADATE ION

ChemComp-HOH:
WATER

ChemComp-ZLJ:
2-chloroethane-1-sulfonic acid

ChemComp-EPE:
4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID / pH buffer*YM

Source
  • saccharolobus solfataricus (archaea)
KeywordsHYDROLASE / protein tyrosine phosphatase / SsoPTP / vanadate / VO4 / 2-chloroethylsuflonate

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