Identification of a hemerythrin-like domain in a P1B-type transport ATPase. Academic Article uri icon

abstract

  • The P(1B)-type ATPases couple the energy of ATP hydrolysis to metal ion translocation across cell membranes. Important for prokaryotic metal resistance and essential metal distribution in eukaryotes, P(1B)-ATPases are divided into subclasses on the basis of their metal substrate specificities. Sequence analysis of putative P(1B-5)-ATPases, for which the substrate has not been identified, led to the discovery of a C-terminal soluble domain homologous to hemerythrin (Hr) proteins and domains. The Hr domain from the Acidothermus cellulolyticus P(1B-5)-ATPase was cloned, expressed, and purified (P(1B-5)-Hr). P(1B-5)-Hr binds two iron ions per monomer and adopts a predominantly helical fold. Optical absorption features of the iron-loaded and azide-treated protein are consistent with features observed for other Hr proteins. Autoxidation to the met form is very rapid, as reported for other prokaryotic Hr domains. The presence of a diiron center was confirmed by electron paramagnetic resonance (EPR) and X-ray absorption spectroscopic (XAS) data. The occurrence of a Hr-like domain in a P-type ATPase is unprecedented and suggests new regulatory mechanisms as well as an expanded function for Hr proteins in biology.

published proceedings

  • Biochemistry

author list (cited authors)

  • Traverso, M. E., Subramanian, P., Davydov, R., Hoffman, B. M., Stemmler, T. L., & Rosenzweig, A. C.

citation count

  • 22

complete list of authors

  • Traverso, Matthew E||Subramanian, Poorna||Davydov, Roman||Hoffman, Brian M||Stemmler, Timothy L||Rosenzweig, Amy C

publication date

  • August 2010