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Structure paper

TitleMolecular Mechanism of Selective Substrate Engagement and Inhibitor Dis-engagement of Cysteine Synthase.
Journal, issue, pagesJ. Biol. Chem., Year 2020
Publish dateMar 23, 2017 (structure data deposition date)
AuthorsKaushik, A. / Rahisuddin, R. / Saini, N. / Singh, R.P. / Kaur, R. / Kaul, S. / Kumaran, S.
External linksJ. Biol. Chem. / PubMed:33162395
MethodsX-ray diffraction
Resolution1.69 - 2.1 Å
Structure data

PDB-5xcn:
Crystal structure of M120A mutant of O-acetyl-L-serine sulfahydrylase from Haemophilus influenzae
Method: X-RAY DIFFRACTION / Resolution: 1.69 Å

PDB-5xcp:
Crystal structure of M92A mutant of O-acetyl-L-serine sulfhydrylase from Haemophilus influenzae
Method: X-RAY DIFFRACTION / Resolution: 2.043 Å

PDB-5xcw:
Crystal structure of M92A-M120A double mutant of O-acetyl-L-serine sulfhydrylase from Haemophilus influenzae
Method: X-RAY DIFFRACTION / Resolution: 1.89 Å

PDB-7c35:
Crystal structure of M96A mutant of O-acetyl-L-serine sulfhydrylase from Haemophilus influenzae
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-7cm8:
High resolution crystal structure of M92A mutant of O-acetyl-L-serine sulfhydrylase from Haemophilus influenzae
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-NA:
Unknown entry

ChemComp-GOL:
GLYCEROL

Source
  • haemophilus influenzae (strain atcc 51907 / dsm 11121 / kw20 / rd) (bacteria)
  • haemophilus influenzae rd kw20 (bacteria)
KeywordsTRANSFERASE / Pyridoxal phosphate binding / cysteine synthase activity / L-cysteine desulfhydrase activity / transferase activity / serine acetyl transferase interacting protein / O-acetylserine (thiol)-lyase / Interacts with Serine acetyl transferase / Serine acetyl transferase binding protein / PLP dependent enzyme / Cysteine metabolizing Enzyme / O acetyl transferase enzyme / Cysteine synthase / Substrate selection / mutant / Competetive allostery

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