Identification of the Transmembrane Metal Binding Site in Cu+-transporting PIB-type ATPases
نویسندگان
چکیده
منابع مشابه
Mechanism of Metal delivery and binding to transport sites of Cu+-transporting ATPases
CopA, a thermophilic membrane ATPase from Archaeoglobus fulgidus, drives the outward movement of Cu across cellular membranes. CopA contains at least two metal binding domains, a regulatory N-terminal Metal Binding Domain (N-MBD) and an occlusion/coordinating metal binding site in the 6, 7 and 8 transmembrane segments. Previous studies showed that the presence of millimolar concentration of Cys...
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Detoxification and homeostatic acquisition of metal ions are vital for all living organisms. We have identified PCA1 in yeast Saccharomyces cerevisiae as an overexpression suppressor of copper toxicity. PCA1 possesses signatures of a P1B-type heavy metal-transporting ATPase that is widely distributed from bacteria to humans. Copper resistance conferred by PCA1 is not dependent on catalytic acti...
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Lactobacillus bulgaricus is a lactic acid bacteria (LAB) that, through the production of lactic acid, gradually acidifies its environment during growth. In the course of this process, L. bulgaricus acquires an improved tolerance to acidity. A survey of the recently established genome sequence shows that this bacterium possesses few of the pH control functions that have been described in other L...
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Powered by ATP hydrolysis, P(IB) -ATPases drive the energetically uphill transport of transition metals. These high affinity pumps are essential for heavy metal detoxification and delivery of metal cofactors to specific cellular compartments. Amino acid sequence alignment of the trans-membrane (TM) helices of P(IB)-ATPases reveals a high degree of conservation, with ∼ 60-70 fully conserved posi...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2004
ISSN: 0021-9258
DOI: 10.1074/jbc.m410854200