Evidence for an ancestral core structure in nucleotide-binding proteins with the type A motif.
Many proteins that bind purine nucleotide triphosphates have a type A sequence motif. Only two classes of structures for such proteins are so far available from X-ray crystallography. We examined the tertiary structures of representatives of the two classes, porcine cytoplasmic adenylate kinase and Escherichia coli translational elongation factor Tu. Comparison of the two proteins suggests that the A motif may be just one part of a larger common core structure consisting of four parallel strands of beta-sheet sandwiched between four alpha-helices. This compact core structure comprises over one half of each protein. We speculate that A motif proteins have diverged from a common ancestor having this core structure.
Milner-White
E J
EJ
Department of Biochemistry, University of Glasgow, Scotland, U.K.
Coggins
J R
JR
Anton
I A
IA
D000263:Adenylate Kinase / Q000737:chemistry* / Q000378:metabolism; D000818:Animals; D002352:Carrier Proteins / Q000737:chemistry* / Q000378:metabolism; D002373:Cyclic AMP Receptor Protein; D004926:Escherichia coli / Q000378:metabolism; D008956:Models, Chemical; D010444:Peptide Elongation Factor Tu / Q000737:chemistry* / Q000378:metabolism; D011487:Protein Conformation; D013552:Swine; D014961:X-Ray Diffraction
D002352:Carrier Proteins; D002373:Cyclic AMP Receptor Protein; D000263:Adenylate Kinase; D010444:Peptide Elongation Factor Tu