Premium
Comparison of the structures of globins and phycocyanins: Evidence for evolutionary relationship
Author(s) -
Pastore Annalisa,
Lesk Arthur M.
Publication year - 1990
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.340080204
Subject(s) - globin , folding (dsp implementation) , evolutionary biology , similarity (geometry) , biology , sequence (biology) , computational biology , helix (gastropod) , protein evolution , function (biology) , genetics , computer science , gene , artificial intelligence , zoology , gastropoda , electrical engineering , image (mathematics) , engineering
Globins and phycocyanins are two classes of proteins with different function, different ligands, and no substantial sequence similarity, yet the conformations of their polypeptide chains show very similar folding patterns. Does this arise from a genuine, albeit very distant, evolutionary relationship, or does it represent a common solution of a structural problem? We address this question by a very detailed comparison of the structures of the two protein families. An analysis of the helices and their interactions shows many features common to globins and phycocyanins, including some exceptional features of the globins such as a 3–10 C helix and the unusual “crossed‐ridge” packing pattern at the B / E helix interfaces. We conclude that the evidence supports the hypothesis of distant evolutionary relationship between globins and phycocyanins.