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Structure paper

TitleMutation of Gly51 to serine in the P-loop of Lactobacillus casei folylpolyglutamate synthetase abolishes activity by altering the conformation of two adjacent loops.
Journal, issue, pagesActa Crystallogr. ,Sect. D, Vol. 62, Page 548-558, Year 2006
Publish dateMar 13, 2006 (structure data deposition date)
AuthorsSmith, C.A. / Cross, J.A. / Bognar, A.L. / Sun, X.
External linksActa Crystallogr. ,Sect. D / PubMed:16627949
MethodsX-ray diffraction
Resolution1.85 - 2.4 Å
Structure data

PDB-2gc5:
G51S mutant of L. casei FPGS
Method: X-RAY DIFFRACTION / Resolution: 1.85 Å

PDB-2gc6:
S73A mutant of L. casei FPGS
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-2gca:
apo form of L. casei FPGS
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

PDB-2gcb:
G51S/S52T double mutant of L. casei FPGS
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

Source
  • lactobacillus casei (bacteria)
KeywordsLIGASE / ATPase / P-loop / site-directed mutant / P-loop enzyme / apo form

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