The role of ligand-containing loops at copper sites in proteins |
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Authors: | Dennison Christopher |
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Affiliation: | Institute for Cell and Molecular Biosciences, Medical School, Newcastle University, Newcastle upon Tyne, UK. christopher.dennison@ncl.ac.uk |
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Abstract: | Many approaches are being used to engineer metalloproteins, with most of these informed by, and aiming to further elucidate, the basic structural requirements for biological metal centers. Cupredoxins are type 1 (T1) copper-containing electron transfer (ET) proteins with a -barrel fold that is thought to constrain metal site structure. The T1 copper ion is bound by ligands mainly originating from a single active site loop whose length and structure varies. This Highlight article will focus on protein engineering studies which have investigated the role of the metal-binding loop for active site integrity and functionality. Scaffold differences are present within the cupredoxin family and their influence has also been assessed. Given the widespread occurrence of -barrel domains in nature, and the array of metal sites in proteins composed of loop regions, the studies described on this model system have implications for a variety of metalloproteins. |
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