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Lookup NU author(s): Professor Christopher Dennison
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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 β-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 β-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. © The Royal Society of Chemistry 2008.
Author(s): Dennison C
Publication type: Review
Publication status: Published
Journal: Natural Product Reports
Year: 2008
Volume: 25
Issue: 1
Pages: 15-24
ISSN (print): 0265-0568
ISSN (electronic): 1460-4752
URL: http://dx.doi.org/10.1039/b707987g
DOI: 10.1039/b707987g
PubMed id: 18250895
