1T3M

Structure of the isoaspartyl peptidase with L-asparaginase activity from E. coli

Summary for 1T3M

• Entry DOI: 10.2210/pdb1t3m/pdb
• Related: 1jn9 1k2x
• Descriptor: Putative L-asparaginase, SODIUM ION, NITRATE ION, ... (5 entities in total)
• Functional Keywords: type iii l-asparaginase, plant-type asparaginase, isoaspartyl peptidase, hydrolase
• Biological source: Escherichia coli; More
• Total number of polymer chains: 4
• Total formula weight: 67788.44

Authors

Prahl, A.,Pazgier, M.,Hejazi, M.,Lockau, W.,Lubkowski, J. (deposition date: 2004-04-27, release date: 2004-07-13, Last modification date: 2023-08-23)

Primary citation

Prahl, A.,Pazgier, M.,Hejazi, M.,Lockau, W.,Lubkowski, J.
Structure of the isoaspartyl peptidase with L-asparaginase activity from Escherichia coli.
Acta Crystallogr.,Sect.D, 60:1173-1176, 2004

PubMed Abstract: The crystal structure of the Escherichia coli enzyme (EcAIII) with isoaspartyl dipeptidase and L-asparaginase activity has been solved and refined to a resolution of 1.65 angstroms, with crystallographic R-factor and Rfree values of 0.178 and 0.209, respectively. EcAIII belongs to the family of N-terminal hydrolases. The amino-acid sequence of EcAIII is homologous to those of putative asparaginases from plants. The structure of EcAIII is similar to the structures of glycosylasparaginases. The mature and catalytically active form of EcAIII is a heterotetramer consisting of two alpha-subunits and two beta-subunits. Both of the equivalent active sites present in the EcAIII tetramer is assisted by a metal-binding site. The metal cations, modelled here as Na+, have not previously been observed in glycosylasparaginases. This reported structure helps to explain the inability of EcAIII and other plant-type asparaginases to hydrolyze N4-(beta-N-acetylglucosaminyl)-L-asparagine, the substrate of glycosylasparaginases.

PubMed: 15159592
DOI: 10.1107/S0907444904003403

Experimental method

X-RAY DIFFRACTION (1.65 Å)