ArticleActa crystallographica. Section D, Structural biology2026
Molecular analysis of 3D domain swapping in the acylphosphatase from Escherichia coli.
Article in Acta crystallographica. Section D, Structural biology, 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
Three-dimensional domain swapping is a mechanism by which proteins form oligomers. At present, the molecular basis that dictates whether some proteins fold in their monomeric form or as intertwined oligomers is poorly understood. Previously, we have described the first intertwined dimer of an acylphosphatase (AcP) from crystals belonging to the orthorhombic space group C222. In this work, we present the first crystallographic structure of monomeric AcP from Escherichia coli (EcoAcP) and compare it with the intertwined structure of the orthorhombic polymorph and a new intertwined dimer structure obtained from crystals belonging to the hexagonal space group P6
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