Isoaspartyl dipeptidase

From Proteopedia

spinqualitylabelsall models E. coli isoaspartyl dipeptidase complex with aspartylhistidine and Zn+2 ions (PDB code 1ybq) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Function Isoaspartyl dipeptidase (IadA) catalyzes the hydrolytic cleavage of L-isoaspartyl (L-β-aspartyl) dipeptides. Used to degrade proteins damaged by L-isoaspartyl residues formation[1]. Structural highlights The of aspartyl dipeptidase contains the substrate and a [2].

3D structures of isoaspartyl dipeptidase

Updated on 12-June-2023

1po9, 1pok, 1onw – EcIadA – Escherichia coli
2aqo, 2aqv – EcIadA (mutant)
5lp3 – EcIadA – Cryo EM
5xgw – CpIadA – Colwellia psychrerythraea
5xgx – CpIadA (mutant)
1ybq – EcIadA (mutant) + β-Asp-His
1poj – EcIadA + inhibitor
1onx – EcIadA + aspartate
7cdh – FiIadA – Fervidobacterium islandicum
7cf6 – FiIadA + β-Asp-Leu
8dqn – IadA – Leucothrix mucor

References

1. ↑ Michalska K, Brzezinski K, Jaskolski M. Crystal structure of isoaspartyl aminopeptidase in complex with L-aspartate. J Biol Chem. 2005 Aug 5;280(31):28484-91. Epub 2005 Jun 9. PMID:15946951 doi:10.1074/jbc.M504501200
2. ↑ Marti-Arbona R, Fresquet V, Thoden JB, Davis ML, Holden HM, Raushel FM. Mechanism of the reaction catalyzed by isoaspartyl dipeptidase from Escherichia coli. Biochemistry. 2005 May 17;44(19):7115-24. PMID:15882050 doi:10.1021/bi050008r