Families of Soft-Metal-Ion-Transporting ATPases
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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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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...
متن کاملMetallochaperones and metal-transporting ATPases: a comparative analysis of sequences and structures.
A comparative structural genomic analysis of a new class of metal-trafficking proteins can provide insights into the intracellular chemistry of reactive cofactors such as copper and zinc. Starting from the sequences of the metallochaperone Atx1 and from the first soluble domain of the copper-transporting ATPase Ccc2, both from yeast, a search on the available genomes was performed using a homol...
متن کاملFunction and regulation of human copper-transporting ATPases.
Copper-transporting ATPases (Cu-ATPases) ATP7A and ATP7B are evolutionarily conserved polytopic membrane proteins with essential roles in human physiology. The Cu-ATPases are expressed in most tissues, and their transport activity is crucial for central nervous system development, liver function, connective tissue formation, and many other physiological processes. The loss of ATP7A or ATP7B fun...
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ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 1999
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.181.19.5891-5897.1999