Fig. 6: Working model of substrate recognition and modification by human OGT. | Nature Communications

Fig. 6: Working model of substrate recognition and modification by human OGT.

From: Cryo-EM structure of human O-GlcNAcylation enzyme pair OGT-OGA complex

Fig. 6: Working model of substrate recognition and modification by human OGT.The alternative text for this image may have been generated using AI.

For clarity, only one OGT monomer (colored in blue) is shown. OGT binds to the intrinsically disordered regions (IDRs) (colored in yellow) of OGA-like substrates through its TPR domain. The superhelical turns of the TPR domain have to partially unwind to allow the IDR to access its lumen. The superhelical turns then reform and wrap around the IDR in a topological embrace, which lengthens the lifetime of the OGT-substrate complex for optimal O-GlcNAcylation. TPR tetratricopeptide repeat, GTD glycosyltransferase domain, IDR intrinsically disordered region.

Back to article page