Crystallographic studies of 3-ketoacylCoA thiolase from yeast Saccharomyces cerevisiae

Zeelen, J.P.; Wierenga, R.K.; Erdmann, Ralf; Kunau, Wolf‐H.

doi:10.1016/s0022-2836(05)80338-9

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Crystallization Data Collection and Heavy Atom Derivatives1

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Cited by 10 publications

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“…The crystals were grown using a microdialysis method [32,33]. The protein solution [5 mg ml -' in a buffer of 200 mM potassium phosphate pH 7.4, 1 mM dithiothreitol (DTT), 1 mM NaN 3 , 1 mM EDTA] was dialyzed against 1 ml of a buffer of 25 mM 3-(N-morpholino)-propanesulfonic acid (MOPS) pH 6.5, 1 mM DTT, NaN 3 , EDTA.…”

Section: Crystallization Data Collection and Heavy Atom Derivativesmentioning

confidence: 99%

The 2.8å Crystal Structure of peroxisomal 3-ketoacyl-CoA thiolase of Saccharomyces cerevisiae : a five-layered αβαβα structure constructed from two core domains of identical topology

et al. 1994

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The crystal structure of thiolase shows that the active site is a shallow pocket, shaped by highly conserved residues. Two conserved cysteines and a histidine at the floor of this pocket probably play key roles in the reaction mechanism. The two active sites are on the same face of the dimer, far from the amino and carboxyl termini of both subunits and the disordered amino-terminal import signal sequence.

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Section: Crystallization Data Collection and Heavy Atom Derivativesmentioning

confidence: 99%