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TitleStructural Snapshots of an Engineered Cystathionine-gamma-lyase Reveal the Critical Role of Electrostatic Interactions in the Active Site.
Journal, issue, pagesBiochemistry, Vol. 56, Page 876-885, Year 2017
Publish dateOct 31, 2016 (structure data deposition date)
AuthorsYan, W. / Stone, E. / Zhang, Y.J.
External linksBiochemistry / PubMed:28106980
MethodsX-ray diffraction
Resolution2.2 - 2.949 Å
Structure data

PDB-5tsu:
Active conformation for Engineered human cystathionine gamma lyase (E59N, R119L, E339V) to depleting methionine
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

PDB-5tt2:
Inactive conformation of engineered human cystathionine gamma lyase (E59N, R119L, E339V) to depleting methionine
Method: X-RAY DIFFRACTION / Resolution: 2.949 Å

Chemicals

ChemComp-MET:
METHIONINE

ChemComp-SO4:
SULFATE ION

ChemComp-LPI:
N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-L-methionine

ChemComp-CYS:
CYSTEINE

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsLYASE / Engineered protein / methioninase / inactive form

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