Functional zinc-binding motifs in enzymes and DNA-binding proteins.
Zinc is now known to be an integral component of a large number and variety of enzymes and proteins involved in virtually all aspects of metabolism, thus accounting for the fact that this element is essential for growth and development. The chemistry of zinc, superficially bland, in reality has turned out to be ideally appropriate and versatile for the unexpected development of multiple and unique chemical structures which biology has used for specific life processes. The present discussion will centre on those distinctive zinc-binding motifs that are critical both to enzyme function and the expression of the genetic message. X-Ray diffraction structure determination of 15 zinc enzymes belonging to IUB classes I-IV provide absolute standards of reference for the identity and nature of zinc ligands in their families. Three types of zinc enzyme binding motifs emerge through analysis of these: catalytic, coactive or cocatalytic, and structural. In contrast to zinc enzymes virtually all DNA-binding proteins contain multiple zinc atoms. With the availability of NMR and X-ray structure analyses three distinct motifs now emerge for those: zinc fingers, twists and clusters.
Vallee
B L
BL
Department of Pathology, Harvard Medical School, Boston, MA 02115.
Auld
D S
DS
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D004268:DNA-Binding Proteins / Q000378:metabolism*; D004798:Enzymes / Q000378:metabolism*; D006801:Humans; D008969:Molecular Sequence Data; D015032:Zinc / Q000378:metabolism*; D016335:Zinc Fingers / Q000502:physiology
D004268:DNA-Binding Proteins; D004798:Enzymes; D015032:Zinc