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Structure paper

TitleStructural analysis of the substrate recognition mechanism in O-phosphoserine sulfhydrylase from the hyperthermophilic archaeon Aeropyrum pernix K1
Journal, issue, pagesJ. Mol. Biol., Vol. 422, Page 33-44, Year 2012
Publish dateApr 24, 2012 (structure data deposition date)
AuthorsNakamura, T. / Kawai, Y. / Kunimoto, K. / Iwasaki, Y. / Nishii, K. / Kataoka, M. / Ishikawa, K.
External linksJ. Mol. Biol. / PubMed:22580223
MethodsX-ray diffraction
Resolution2.07 - 2.09 Å
Structure data

PDB-3vsa:
Crystal Structure of O-phosphoserine sulfhydrylase without acetate
Method: X-RAY DIFFRACTION / Resolution: 2.07 Å

PDB-3vsc:
Crystal Structure of the K127A Mutant of O-Phosphoserine Sulfhydrylase Complexed with External Schiff Base of Pyridoxal 5'-Phosphate with O-Phospho-L-Serine
Method: X-RAY DIFFRACTION / Resolution: 2.07 Å

PDB-3vsd:
Crystal Structure of the K127A Mutant of O-Phosphoserine Sulfhydrylase Complexed with External Schiff Base of Pyridoxal 5'-Phosphate with O-Acetyl-L-Serine
Method: X-RAY DIFFRACTION / Resolution: 2.09 Å

Chemicals

ChemComp-PLP:
PYRIDOXAL-5'-PHOSPHATE

ChemComp-MPD:
(4S)-2-METHYL-2,4-PENTANEDIOL / precipitant*YM

ChemComp-HOH:
WATER

ChemComp-SEP:
PHOSPHOSERINE

ChemComp-OAS:
O-ACETYLSERINE

Source
  • aeropyrum pernix (archaea)
KeywordsTRANSFERASE / Cysteine Biosynthesis / Internal Schiff base / sulfhydrylase / External Schiff base of PLP with O-phosphoserine / K127A mutant / sulfhydrylase (inactivated) / External Schiff base of PLP with O-acetylserine

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