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- W4229724081 abstract "The α-D-phosphohexomutase superfamily comprises enzymes involved in carbohydrate metabolism that are found in all kingdoms of life. Recent biophysical studies have shown for the first time that several of these enzymes exist as dimers in solution, prompting an examination of the oligomeric state of all proteins of known structure in the superfamily (11 different proteins; 31 crystal structures) via computational and experimental analyses. We find that these proteins range in quaternary structure from monomers to tetramers, with six of the 11 known structures being likely oligomers. The oligomeric state of these proteins is associated in some cases with enzyme sub-group (i.e. substrate specificity), but also appears to depend on domain of life, with the two archaeal proteins existing as higher order oligomers. within the oligomers, three distinct interfaces are observed, one of which is found in both archaeal and bacterial proteins. Normal mode analysis shows that the topological arrangement of the oligomers permits domain 4 of each protomer to move independently as required for catalysis. Our analysis suggests that the advantages associated with protein flexibility in this enzyme family are of sufficient importance to be maintained during the evolution of multiple independent oligomers. This study is one of the first showing that global motions are conserved not only within protein families, but across members of a superfamily with varying oligomeric structures. Correction et al.Biophysical JournalApril 16, 2013In Brief2013. Conservation of Functionally Important Global Motions in an Enzyme Superfamily across Varying Quaternary Structures. Emily K. Luebbering. Biophys. J. 104(2)s: 569a. Full-Text PDF Open Archive" @default.
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- W4229724081 date "2013-01-01" @default.
- W4229724081 modified "2023-09-27" @default.
- W4229724081 title "Conservation of Functionally Important Global Motions in an Enzyme Superfamily across Varying Quaternary Structures" @default.
- W4229724081 doi "https://doi.org/10.1016/j.bpj.2012.11.3158" @default.
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