3HQN

Apo crystal structure of Leishmania mexicana(LmPYK)pyruvate kinase

Summary for 3HQN

• Entry DOI: 10.2210/pdb3hqn/pdb
• Related: 1PKL 3E0V 3E0W 3HQO 3HQP 3HQQ
• Descriptor: Pyruvate kinase, GLYCEROL, SULFATE ION, ... (5 entities in total)
• Functional Keywords: tim barrel, t-state enzyme, 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: 109560.67

Authors

Morgan, H.P.,Walkinshaw, M.D. (deposition date: 2009-06-08, release date: 2010-02-16, Last modification date: 2023-11-01)

Primary citation

Morgan, H.P.,McNae, I.W.,Nowicki, M.W.,Hannaert, V.,Michels, P.A.M.,Fothergill-Gilmore, L.A.,Walkinshaw, M.D.
The allosteric mechanism of pryuvate kinase from Leishmania mexicana: a rock and lock model
J.Biol.Chem., 285:12892-12898, 2010

PubMed Abstract: Allosteric regulation provides a rate management system for enzymes involved in many cellular processes. Ligand-controlled regulation is easily recognizable, but the underlying molecular mechanisms have remained elusive. We have obtained the first complete series of allosteric structures, in all possible ligated states, for the tetrameric enzyme, pyruvate kinase, from Leishmania mexicana. The transition between inactive T-state and active R-state is accompanied by a simple symmetrical 6 degrees rigid body rocking motion of the A- and C-domain cores in each of the four subunits. However, formation of the R-state in this way is only part of the mechanism; eight essential salt bridge locks that form across the C-C interface provide tetramer rigidity with a coupled 7-fold increase in rate. The results presented here illustrate how conformational changes coupled with effector binding correlate with loss of flexibility and increase in thermal stability providing a general mechanism for allosteric control.

PubMed: 20123988
DOI: 10.1074/jbc.M109.079905

Experimental method

X-RAY DIFFRACTION (2 Å)