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TitleThe differential ability of asparagine and glutamine in promoting the closed/active enzyme conformation rationalizes the Wolinella succinogenes L-asparaginase substrate specificity.
Journal, issue, pagesSci Rep, Vol. 7, Page 41643-41643, Year 2017
Publish dateMay 19, 2016 (structure data deposition date)
AuthorsNguyen, H.A. / Durden, D.L. / Lavie, A.
External linksSci Rep / PubMed:28139703
MethodsX-ray diffraction
Resolution1.6 - 2 Å
Structure data

PDB-5k3o:
Wolinella succinogenes L-asparaginase P121 and L-Aspartic acid
Method: X-RAY DIFFRACTION / Resolution: 1.696 Å

PDB-5k45:
Wolinella succinogenes L-asparaginase P121 + L-Glutamic acid
Method: X-RAY DIFFRACTION / Resolution: 1.63 Å

PDB-5k4g:
Wolinella succinogenes L-asparaginase S121 + L-aspartic acid, open conformation
Method: X-RAY DIFFRACTION / Resolution: 1.6 Å

PDB-5k4h:
Wolinella succinogenes L-asparaginase S121 + L-Glutamic acid
Method: X-RAY DIFFRACTION / Resolution: 2 Å

Chemicals

ChemComp-ASP:
ASPARTIC ACID

ChemComp-HOH:
WATER

ChemComp-GLU:
GLUTAMIC ACID

Source
  • wolinella succinogenes (strain atcc 29543 / dsm 1740 / lmg 7466 / nctc 11488 / fdc 602w) (bacteria)
KeywordsHYDROLASE / L-asparaginase / P121 / L-aspartic acid / L-glutamic acid / S121 / open conformation

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