The linked conservation of structure and function in a family of high diversity: the monomeric cupredoxins

J. Gough, C. Chothia

Research output: Contribution to journalArticle (Academic Journal)

27 Citations (Scopus)

Abstract

The monomeric cupredoxins are a highly divergent family of copper binding electron transport proteins that function in photosynthesis and respiration. To determine how function and structure are conserved in the context of large sequence differences, we have carried out a detailed analysis of the cupredoxins of known structure and their sequence homologs. The common structure of the cupredoxins is formed by a sandwich of two beta sheets which support a copper binding site. The structure of the deeply buried core is intimately coupled to the binding site on the surface of the protein; in each protein the conserved regions form one continuous substructure that extends from the surface active site and through the center of the molecule. Residues around the active site are conserved for functional reasons, while those deeper in the structure will be conserved for structural reasons. Together the two sets support each other.
Translated title of the contributionThe linked conservation of structure and function in a family of high diversity: the monomeric cupredoxins
Original languageEnglish
Article number917-925
JournalStructure
Volume12
Publication statusPublished - 2004

Bibliographical note

Other identifier: 1040012

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