Fig. 3: ABE8e was chosen for investigating the influences of REC expansion on N-end catalytic domain. | Nature Communications

Fig. 3: ABE8e was chosen for investigating the influences of REC expansion on N-end catalytic domain.

From: Improving adenine base editing precision by enlarging the recognition domain of CRISPR-Cas9

Fig. 3

a Protein structure of FnCas9 and ABE8e. Left, FnCas9 (PDB 5b2o); right, ABE8e (PDB 6vpc) contains an engineered deoxyadenosine deaminase TadA from Escherichia coli and a nickase SpCas9 (D10A). b Hypothetical model of REC expansion for Cas9 fusion. In this proposed model, the insertion may lead to a rearrangement of the original REC domain and shorten the distance between REC and TadA by enlarging the coverage of the engineered REC lobe, thereby generating additional interactions between these two domains.

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