9XG1
Crystal structure of protein-asparaginase from Amycolatopsis deserti
Summary for 9XG1
| Entry DOI | 10.2210/pdb9xg1/pdb |
| Descriptor | Protein-asparaginase (2 entities in total) |
| Functional Keywords | protein asparaginase, hydrolase |
| Biological source | Amycolatopsis deserti |
| Total number of polymer chains | 1 |
| Total formula weight | 82040.50 |
| Authors | |
| Primary citation | Ono, T.,Yamaguchi, H.,Takahashi, K.,Hirao, Y.,Abe, I.,Chisuga, T.,Fujinami, D.,Nakano, S.,Ito, S. Structural and Biochemical Characterization of a Minimal Protein-Asparaginase. Chembiochem, 27:e202500893-e202500893, 2026 Cited by PubMed Abstract: Enzymatic deamidation of proteins, catalyzed by protein glutaminase (PG) for Gln or by protein asparaginase (PA) for Asn residues, is a key strategy for improving functional properties such as solubility and foaming. However, the only known PA, from Luteimicrobium album (LalPA), is a large, thermally unstable multidomain protein (1355 aa) that has proven challenging to express heterologously. To overcome these limitations, we identified a novel, compact PA from Amycolatopsis deserti (AdePA) using a comprehensive database search. We then solved the first experimental structure of any PA, which revealed a catalytic mechanism utilizing a Ser-His-Asp catalytic triad indicative of a serine protease-like function, which is distinct from that of L-asparaginase. AdePA offers significant advantages over LalPA; it is a smaller (785 aa) single-domain enzyme with superior thermal stability (retaining 50% activity at 40°C, where LalPA is inactivated) and is readily produced through heterologous expression. Furthermore, AdePA shows inverted substrate specificity, preferring sterically small N-terminal groups, making it highly effective for modifying unstructured proteins like gelatin. These findings demonstrate that AdePA is a robust candidate for industrial applications in protein modification. PubMed: 41704006DOI: 10.1002/cbic.202500893 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.08 Å) |
Structure validation
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