3KTX

Crystal structure of Leishmania mexicana pyruvate kinase (LmPYK)in complex with 1,3,6,8-pyrenetetrasulfonic acid

Summary for 3KTX

• Entry DOI: 10.2210/pdb3ktx/pdb
• Related: 1PKL
• Descriptor: Pyruvate kinase, GLYCEROL, pyrene-1,3,6,8-tetrasulfonic acid, ... (4 entities in total)
• Functional Keywords: transferase, allosteric enzyme, atp-binding, glycolysis, kinase, magnesium, metal-binding, nucleotide-binding, pyruvate
• Biological source: Leishmania mexicana
• Total number of polymer chains: 2
• Total formula weight: 110010.93

Authors

Morgan, H.P.,Walkinshaw, M.D. (deposition date: 2009-11-26, release date: 2010-02-09, Last modification date: 2023-09-06)

Primary citation

Morgan, H.P.,McNae, I.W.,Hsin, K.Y.,Michels, P.A.,Fothergill-Gilmore, L.A.,Walkinshaw, M.D.
An improved strategy for the crystallization of Leishmania mexicana pyruvate kinase.
Acta Crystallogr.,Sect.F, 66:215-218, 2010

PubMed Abstract: The inclusion of novel small molecules in crystallization experiments has provided very encouraging results and this method is now emerging as a promising alternative strategy for crystallizing 'problematic' biological macromolecules. These small molecules have the ability to promote lattice formation through stabilizing intermolecular interactions in protein crystals. Here, the use of 1,3,6,8-pyrenetetrasulfonic acid (PTS), which provides a helpful intermolecular bridge between Leishmania mexicana PYK (LmPYK) macromolecules in the crystal, is reported, resulting in the rapid formation of a more stable crystal lattice at neutral pH and greatly improved X-ray diffraction results. The refined structure of the LmPYK-PTS complex revealed the negatively charged PTS molecule to be stacked between positively charged (surface-exposed) arginine side chains from neighbouring LmPYK molecules in the crystal lattice.

PubMed: 20208146
DOI: 10.1107/S1744309109053494

Experimental method

X-RAY DIFFRACTION (2.1 Å)