Inhibition of a Cl−- Transporting P-type ATPase in Aplysia Gut
نویسندگان
چکیده
منابع مشابه
Nucleotide recognition by CopA, a Cu+-transporting P-type ATPase.
Heavy metal pumps constitute a large subgroup in P-type ion-transporting ATPases. One of the outstanding features is that the nucleotide binding N-domain lacks residues critical for ATP binding in other well-studied P-type ATPases. Instead, they possess an HP-motif and a Gly-rich sequence in the N-domain, and their mutations impair ATP binding. Here, we describe 1.85 A resolution crystal struct...
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ii DEDICATION iv ACKNOWLEDGEMENTS v TABLE OF CONTENTS vi ABBREVIATIONS xii Chapter
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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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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...
متن کاملMembrane structure of CtrA3, a copper-transporting P-type-ATPase from Aquifex aeolicus.
We have produced and characterized two new copper-transporting ATPases, CtrA2 and CtrA3 from Aquifex aeolicus, that belong to the family of heavy metal ion-transporting P(IB)-type ATPases. CtrA2 has a CPC metal-binding sequence in TM6 and a CxxC metal-binding N-terminal domain, while CtrA3 has a CPH metal-binding motif in TM6 and a histidine-rich N-terminal metal-binding domain. We have cloned ...
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ژورنال
عنوان ژورنال: Zoological Science
سال: 2001
ISSN: 0289-0003
DOI: 10.2108/zsj.18.17