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TitleA pH-dependent stabilization of an active site loop observed from low and high pH crystal structures of mutant monomeric glycinamide ribonucleotide transformylase at 1.8 to 1.9 A.
Journal, issue, pagesJ. Mol. Biol., Vol. 281, Page 485-499, Year 1998
Publish dateMay 13, 1998 (structure data deposition date)
AuthorsSu, Y. / Yamashita, M.M. / Greasley, S.E. / Mullen, C.A. / Shim, J.H. / Jennings, P.A. / Benkovic, S.J. / Wilson, I.A.
External linksJ. Mol. Biol. / PubMed:9698564
MethodsX-ray diffraction
Resolution1.8 - 1.9 Å
Structure data

PDB-2gar:
A PH-DEPENDENT STABLIZATION OF AN ACTIVE SITE LOOP OBSERVED FROM LOW AND HIGH PH CRYSTAL STRUCTURES OF MUTANT MONOMERIC GLYCINAMIDE RIBONUCLEOTIDE TRANSFORMYLASE
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-3gar:
A PH-DEPENDENT STABLIZATION OF AN ACTIVE SITE LOOP OBSERVED FROM LOW AND HIGH PH CRYSTAL STRUCTURES OF MUTANT MONOMERIC GLYCINAMIDE RIBONUCLEOTIDE TRANSFORMYLASE
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

Chemicals

ChemComp-PO4:
PHOSPHATE ION

ChemComp-HOH:
WATER

Source
  • escherichia coli (E. coli)
KeywordsPURINE BIOSYNTHESIS / FOLATE COFACTORS / LOOP FLEXIBILITY / MONOMER-DIMER ASSOCIATION / ENZYME MECHANISM / ANTI-CANCER AGENTS

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