9PGZ
X-ray crystal structure of SRD42
Summary for 9PGZ
| Entry DOI | 10.2210/pdb9pgz/pdb |
| Descriptor | Tyrosinase,Tyrosine-protein kinase Fyn, ZINC ION (3 entities in total) |
| Functional Keywords | tyrosinase, chimera, transferase |
| Biological source | Priestia megaterium More |
| Total number of polymer chains | 1 |
| Total formula weight | 40516.65 |
| Authors | Kuzelka, K.P.,Nair, S.K. (deposition date: 2025-07-08, release date: 2025-12-24, Last modification date: 2025-12-31) |
| Primary citation | Shelby, C.,Kuzelka, K.P.,Ellis, J.M.,Yao, Z.,McCue, A.C.,Park, R.,Nair, S.K.,Bowers, A.,Kuhlman, B. Enhancing enzymatic bioconjugation efficiency via installation of a substrate recruitment domain. Biorxiv, 2025 Cited by PubMed Abstract: Enzyme mediated bioconjugation provides a method for easy and rapid formation of protein-protein and protein-small molecule conjugates under mild conditions. Promiscuous enzymes are of particular interest because they can catalyze conjugation reactions on a broad set of substrates. However, this promiscuity carries the risk of undesirable off-target modifications. To mitigate this effect, we used computational design to install a substrate recruitment domain (SRD) onto the promiscuous enzyme, tyrosinase. The redesigned tyrosinase, called D42, preferentially modifies tyrosine residues within the peptide core (core) linked to a 6-amino acid recognition motif/sequence (RS) specific for the SRD. Incorporation of the recognition sequence along with a neighboring tyrosine in peptides or proteins allows for rapid D42-mediated conversion of the tyrosine to an orthoquinone, which can be selectively modified with a variety of nucleophiles. We demonstrate the utility of our design system by rapidly installing cytotoxic molecules on a monoclonal antibody. PubMed: 41279480DOI: 10.1101/2025.10.27.684804 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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