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Science 20 December 1991:
Vol. 254. no. 5039, pp. 1776 - 1779
DOI: 10.1126/science.1763327
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Articles

Science, Vol 254, Issue 5039, 1776-1779
Copyright © 1991 by American Association for the Advancement of Science

articles

Identification and characterization of zinc binding sites in protein kinase C

Hubbard SR, WR Bishop, P Kirschmeier, SJ George, SP Cramer, and WA Hendrickson

Howard Hughes Medical Institute, New York, NY.

Metal ion coordination in the regulatory domain of protein kinase C (PKC) is suggested by the conservation of six cysteines and two histidines in two homologous regions found therein. By monitoring x-ray fluorescence from a purified sample of rat PKC beta I overexpressed in insect cells, direct evidence has been obtained that PKC beta I tightly binds four zinc ions (Zn2+) per molecule. Extended x-ray absorption fine structure (EXAFS) data are best fit by an average Zn2+ coordination of one nitrogen and three sulfur atoms. Of the plausible Zn2+ coordination models, only those featuring nonbridged Zn2+ sites accommodate the EXAFS data and all of the conserved potential ligands.


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Science. ISSN 0036-8075 (print), 1095-9203 (online)