5B59

Hen egg-white lysozyme modified with a keto-ABNO.

Summary for 5B59

• Entry DOI: 10.2210/pdb5b59/pdb
• Descriptor: Lysozyme C, (1~{S},5~{R})-9-oxidanyl-9-azabicyclo[3.3.1]nonan-3-one (3 entities in total)
• Functional Keywords: catalyst, modification, hydrolase
• Biological source: Gallus gallus (chicken)
• Cellular location: Secreted: P00698
• Total number of polymer chains: 1
• Total formula weight: 14502.35

Authors

Sasaki, D.,Seki, Y.,Sohma, Y.,Oisaki, K.,Kanai, M. (deposition date: 2016-04-28, release date: 2016-09-14, Last modification date: 2024-11-06)

Primary citation

Seki, Y.,Ishiyama, T.,Sasaki, D.,Abe, J.,Sohma, Y.,Oisaki, K.,Kanai, M.
Transition Metal-Free Tryptophan-Selective Bioconjugation of Proteins
J.Am.Chem.Soc., 138:10798-10801, 2016

PubMed Abstract: Chemical modifications of native proteins can facilitate production of supernatural protein functions that are not easily accessible by complementary methods relying on genetic manipulations. However, accomplishing precise control over selectivity while maintaining structural integrity and homogeneity still represents a formidable challenge. Herein, we report a transition metal-free method for tryptophan-selective bioconjugation of proteins that is based on an organoradical and operates under ambient conditions. This method exhibits low levels of cross-reactivity and leaves higher-order structures of the protein and various functional groups therein unaffected. The strategy to target less abundant amino acids contributes to the formation of structurally homogeneous conjugates, which may even be suitable for protein crystallography. The absence of toxic metals and biochemically incompatible conditions allows a rapid functional modulation of native proteins such as antibodies and pathogenic aggregative proteins, and this method may thus easily find therapeutic applications.

PubMed: 27534812
DOI: 10.1021/jacs.6b06692

Experimental method

X-RAY DIFFRACTION (2 Å)