TY - JOUR
T1 - Crystal packing of plant-type L-asparaginase from Escherichia coli
AU - Michalska, Karolina
AU - Borek, Dominika
AU - Hernändez-Santoyo, Alejadra
AU - Jaskolski, Mariusz
PY - 2008/2/20
Y1 - 2008/2/20
N2 - Plant-type L-asparaginases hydrolyze the side-chain amide bond of L-asparagine or its β-peptides. They belong to the N-terminal nucleophile (Ntn) hydrolases and are synthesized as inactive precursor molecules. Activation occurs via the autoproteolytic release of two subunits, α and β, the latter of which carries the nucleophile at its N-terminus. Crystallo-graphic studies of plant-type asparaginases have focused on an Escherichia coli homologue (EcAIII), which has been crystallized in several crystal forms. Although they all belong to the same P212121 space group with similar unit-cell parameters, they display different crystaL-packing arrangements and thus should be classified as separate polymorphs. This variability stems mainly from different positions of the EcAIII molecules within the unit cell, although they also exhibit slight differences in orientation. The intermolecular interactions that trigger different crystal lattice formation are mediated by ions, which represent the most variable component of the crystallization conditions. This behaviour confirms recent observations that small molecules might promote protein crystal lattice formation.
AB - Plant-type L-asparaginases hydrolyze the side-chain amide bond of L-asparagine or its β-peptides. They belong to the N-terminal nucleophile (Ntn) hydrolases and are synthesized as inactive precursor molecules. Activation occurs via the autoproteolytic release of two subunits, α and β, the latter of which carries the nucleophile at its N-terminus. Crystallo-graphic studies of plant-type asparaginases have focused on an Escherichia coli homologue (EcAIII), which has been crystallized in several crystal forms. Although they all belong to the same P212121 space group with similar unit-cell parameters, they display different crystaL-packing arrangements and thus should be classified as separate polymorphs. This variability stems mainly from different positions of the EcAIII molecules within the unit cell, although they also exhibit slight differences in orientation. The intermolecular interactions that trigger different crystal lattice formation are mediated by ions, which represent the most variable component of the crystallization conditions. This behaviour confirms recent observations that small molecules might promote protein crystal lattice formation.
KW - Asparaginases
KW - Crystal packing
KW - Isoaspartyl peptidases
KW - Ntn hydrolases
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U2 - 10.1107/S0907444907068072
DO - 10.1107/S0907444907068072
M3 - Article
C2 - 18323626
AN - SCOPUS:40449100981
VL - 64
SP - 309
EP - 320
JO - Acta Crystallographica Section D: Structural Biology
JF - Acta Crystallographica Section D: Structural Biology
SN - 0907-4449
IS - 3
ER -