title: The role of ligand-containing loops at copper sites in proteins.
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.
authors.affiliation: Institute for Cell and Molecular Biosciences, Medical School, Newcastle University, Newcastle upon Tyne, UK. christopher.dennison@ncl.ac.uk
authors.forename: Christopher
authors.initials: C
authors.lastname: Dennison
mesh_terms: D001400:Azurin / Q000737:chemistry*; D003300:Copper / Q000737:chemistry* / Q000378:metabolism*; D008024:Ligands; D008667:Metalloproteins / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D011487:Protein Conformation; D011550:Pseudomonas aeruginosa / Q000235:genetics / Q000378:metabolism
chemical_list: D008024:Ligands; D008667:Metalloproteins; C050107:cupredoxin; D001400:Azurin; D003300:Copper