ArticleActa crystallographica. Section F, Structural biology communications2026
Crystal structures of PCNA1 and PCNA2 from Aeropyrum pernix: implications for a distorted heterotrimeric sliding clamp.
Article in Acta crystallographica. Section F, Structural biology communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Aeropyrum pernix is a hyperthermophilic archaeon that possesses three proliferating cell nuclear antigen (PCNA) isoforms (ApePCNA1, ApePCNA2 and ApePCNA3) that form a heterotrimeric sliding clamp. To gain more detailed structural insights into this heterotrimeric assembly, we determined the crystal structures of ApePCNA1 and ApePCNA2. ApePCNA1 was crystallized under a new condition, and the 1.60 Å resolution structure revealed a unique nonproline cis-peptide bond between Arg187 and Arg188, which was not deeply discussed in a previous report. The structure of ApePCNA2 was determined at 2.17 Å resolution, and it forms a typical homotrimeric ring. In the cubic crystal form, its crystal packing shows an intriguing tetrahedral assembly of four trimers. Modeling the ApePCNA1-ApePCNA2-ApePCNA3 heterotrimer based on these structures suggests that the cis-peptide in ApePCNA1 induces significant steric hindrance at the subunit interface, leading to a symmetry-broken or distorted ring conformation rather than the canonical pseudo-threefold-symmetric assembly.
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