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Structure paper

TitleActive site coupling in Plasmodium falciparum GMP synthetase is triggered by domain rotation.
Journal, issue, pagesNat Commun, Vol. 6, Page 8930-8930, Year 2015
Publish dateSep 26, 2014 (structure data deposition date)
AuthorsBallut, L. / Violot, S. / Shivakumaraswamy, S. / Thota, L.P. / Sathya, M. / Kunala, J. / Dijkstra, B.W. / Terreux, R. / Haser, R. / Balaram, H. / Aghajari, N.
External linksNat Commun / PubMed:26592566
MethodsX-ray diffraction
Resolution2.6 - 3.6 Å
Structure data

PDB-4wim:
Crystal Structure of the GMP Synthetase from Plasmodium falciparum
Method: X-RAY DIFFRACTION / Resolution: 3.6 Å

PDB-4win:
Crystal structure of the GATase domain from Plasmodium falciparum GMP synthetase
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

PDB-4wio:
Crystal structure of the C89A GMP synthetase inactive mutant from Plasmodium falciparum in complex with glutamine
Method: X-RAY DIFFRACTION / Resolution: 3.15 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-NO3:
NITRATE ION

ChemComp-GLN:
GLUTAMINE

Source
  • plasmodium falciparum 3d7 (eukaryote)
  • plasmodium falciparum (malaria parasite P. falciparum)
KeywordsLYASE / GMP synthetase / purine salvage pathway / TRANSFERASE / Plasmodium falciparum / glutamine amidotransferase / LIGASE

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