9xg1

Crystal structure of protein-asparaginase from Amycolatopsis deserti

spinqualitylabelsall models 9xg1, resolution 2.08Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9xg1 is a 1 chain structure with sequence from Amycolatopsis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.08Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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 degrees 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. Structural and Biochemical Characterization of a Minimal Protein-Asparaginase.,Ono T, Yamaguchi H, Takahashi K, Hirao Y, Abe I, Chisuga T, Fujinami D, Nakano S, Ito S Chembiochem. 2026 Feb 25;27(4):e202500893. doi: 10.1002/cbic.202500893. PMID:41704006 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA