2ZAL
Crystal structure of E. coli isoaspartyl aminopeptidase/L-asparaginase in complex with L-aspartate
Replaces: 1SEOSummary for 2ZAL
| Entry DOI | 10.2210/pdb2zal/pdb |
| Related | 1APY 1APZ 1AYY 1JN9 1K2X 1P4V 1T3M 2GAC 2GAW 9GAA 9GAC 9GAF |
| Descriptor | L-asparaginase, SODIUM ION, CALCIUM ION, ... (8 entities in total) |
| Functional Keywords | isoaspartyl peptidase, asparaginase, ntn-hydrolase, autoproteolysis, l-aspartate/calcium cluster, hydrolase |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 4 |
| Total formula weight | 62959.70 |
| Authors | Michalska, K.,Brzezinski, K.,Jaskolski, M. (deposition date: 2007-10-07, release date: 2007-10-30, Last modification date: 2023-11-01) |
| Primary citation | Michalska, K.,Brzezinski, K.,Jaskolski, M. Crystal structure of isoaspartyl aminopeptidase in complex with L-aspartate J.Biol.Chem., 280:28484-28491, 2005 Cited by PubMed Abstract: The crystal structure of Escherichia coli isoaspartyl aminopeptidase/asparaginase (EcAIII), an enzyme belonging to the N-terminal nucleophile (Ntn)-hydrolases family, has been determined at 1.9-A resolution for a complex obtained by cocrystallization with l-aspartate, which is a product of both enzymatic reactions catalyzed by EcAIII. The enzyme is a dimer of heterodimers, (alphabeta)(2). The (alphabeta) heterodimer, which arises by autoproteolytic cleavage of the immature protein, exhibits an alphabetabetaalpha-sandwich fold, typical for Ntn-hydrolases. The asymmetric unit contains one copy of the EcAIII.Asp complex, with clearly visible l-aspartate ligands, one bound in each of the two active sites of the enzyme. The l-aspartate ligand is located near Thr(179), the N-terminal residue of subunit beta liberated in the autoproteolytic event. Structural comparisons with the free form of EcAIII reveal that there are no major rearrangements of the active site upon aspartate binding. Although the ligand binding mode is similar to that observed in an l-aspartate complex of the related enzyme human aspartylglucosaminidase, the architecture of the EcAIII active site sheds light on the question of substrate specificity and explains why EcAIII is not able to hydrolyze glycosylated asparagine substrates. PubMed: 15946951DOI: 10.1074/jbc.M504501200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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