Structural drift: a possible path to protein fold change.
CONCLUSIONS
Along with their mutating sequences, protein structures change in time. Analyzing a formate dehydrogenase domain that is evolutionarily related to ferredoxin, but simultaneously contains all the structural elements of a beta-Grasp fold, we illustrate here a mechanism termed as structural drift, by which changes to a protein fold can occur.


BACKGROUND
grishin@chop.swmed.edu.
Krishna
S Sri
SS
Howard Hughes Medical Institute, University of Texas Southwestern Medical Center, 5323, Harry Hines Blvd, Dallas, TX 75390-9050, USA.
Grishin
Nick V
NV
D002352:Carrier Proteins / Q000737:chemistry / Q000235:genetics; D019143:Evolution, Molecular; D005288:Ferredoxins / Q000737:chemistry* / Q000235:genetics*; D005560:Formate Dehydrogenases / Q000737:chemistry* / Q000235:genetics*; D040961:Genetic Drift; D008565:Membrane Proteins; D008956:Models, Chemical; D008958:Models, Molecular; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D021122:Protein Subunits; D020539:Sequence Analysis, Protein / Q000379:methods*; D013329:Structure-Activity Relationship
D002352:Carrier Proteins; D005288:Ferredoxins; D008565:Membrane Proteins; D021122:Protein Subunits; C410230:tamalin protein, human; D005560:Formate Dehydrogenases