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. 2016 May 3;44(13):6232–6241. doi: 10.1093/nar/gkw351

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Published by Oxford University Press on behalf of Nucleic Acids Research 2016. This work is written by (a) US Government employee(s) and is in the public domain in the US.

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Figure 5. — TIP binding breaks the interface between monomers of PCNA. (A) The interface between monomers of the trimer ring in free PCNA involves a smooth continuation of the β-sheets (cyan to tan). (B) The twist of domain I in the PCNA:TIP structure prevents trimer formation. To create panel B, the domain II of PCNA:TIP (blue:gold) has been superimposed onto the domain II of one of the monomers in the free PCNA trimer (cyan), then that free PCNA domain was removed from the graphic. The β-strands (from blue to tan) no longer line up to form a hydrogen bonded continuous sheet. The C-terminal end of TIP is fairly flexible since residues 57–61 have higher average B-factors.