1K2X
Crystal structure of putative asparaginase encoded by Escherichia coli ybiK gene
Summary for 1K2X
| Entry DOI | 10.2210/pdb1k2x/pdb |
| Related | 1APY 1APZ 1AYY 1JN9 2GAC 2GAW 9GAA 9GAC 9GAF |
| Descriptor | Putative L-asparaginase, SODIUM ION, CHLORIDE ION, ... (5 entities in total) |
| Functional Keywords | ntn hydrolase, asparginase, autoproteolysis, hydrolase |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 4 |
| Total formula weight | 67138.74 |
| Authors | Borek, D.,Jaskolski, M. (deposition date: 2001-09-30, release date: 2003-09-09, Last modification date: 2023-08-16) |
| Primary citation | Michalska, K.,Borek, D.,Hernandez-Santoyo, A.,Jaskolski, M. Crystal packing of plant-type L-asparaginase from Escherichia coli. Acta Crystallogr.,Sect.D, 64:309-320, 2008 Cited by PubMed Abstract: Plant-type L-asparaginases hydrolyze the side-chain amide bond of L-asparagine or its beta-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, alpha and beta, the latter of which carries the nucleophile at its N-terminus. Crystallographic 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 P2 1 2 1 2 1 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. PubMed: 18323626DOI: 10.1107/S0907444907068072 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.65 Å) |
Structure validation
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