P-type ATPases and their role in metal homeostasis in plants

Keeran, Nisha S.; Balasundaram, Usha; Govindan, Ganesan

doi:10.1016/b978-0-12-817955-0.00002-8

Cited by 3 publications

(3 citation statements)

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“…4 , Table 3 ). 54 , 55 The P1B class of P-type ATPases uses the energy of ATP hydrolysis to transport d-block metal ions across cell membranes. In plants, the P1B class of P-type ATPases are key components in the maintenance of metal homeostasis, with characterized transporters for Zn 2+ , Cu 2+ , Cd 2+ , Co 2+ , and Pb 2+ ions.…”

Section: Atpase Metallotransporters and Metallochaperonesmentioning

confidence: 99%

“…In plants, the P1B class of P-type ATPases are key components in the maintenance of metal homeostasis, with characterized transporters for Zn 2+ , Cu 2+ , Cd 2+ , Co 2+ , and Pb 2+ ions. 54 These transporters serve as the first step in metalloprotein maturation by acquiring d-block metal ions from the surrounding environment. Analogous to the P-loop GTPases described above, P-loop ATPases are also involved in transporting metal ions to the active site of their target protein.…”

Section: Atpase Metallotransporters and Metallochaperonesmentioning

confidence: 99%

“…The flux of heavy metals is coupled to the hydrolysis of ATP. 54 (B) The heat shock protein fold ATPases, such as HscA from E. coli (PDB 1U00), interact with co-chaperones in a nucleotide-dependent manner to transfer newly synthesized [2Fe-2S] clusters in the ISC biogenesis pathway. 100 …”

Section: Atpase Metallotransporters and Metallochaperonesmentioning

confidence: 99%

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The role of nucleoside triphosphate hydrolase metallochaperones in making metalloenzymes

Vaccaro

Drennan

2022

Metallomics

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Metalloenzymes catalyze a diverse set of challenging chemical reactions that are essential for life. These metalloenzymes rely on a wide range of metallocofactors, from single metal ions to complicated metallic clusters. Incorporation of metal ions and metallocofactors into apo-proteins often requires the assistance of proteins known as metallochaperones. Nucleoside triphosphate hydrolases (NTPases) are one important class of metallochaperones and are found widely distributed throughout the domains of life. These proteins use the binding and hydrolysis of nucleoside triphosphates, either adenosine triphosphate (ATP) or guanosine triphosphate (GTP), to carry out highly specific and regulated roles in the process of metalloenzyme maturation. Here, we review recent literature on NTPase metallochaperones and describe the current mechanistic proposals and available structural data. By using representative examples from each type of NTPase, we also illustrate the challenges in studying these complicated systems. We highlight open questions in the field and suggest future directions. This minireview is part of a special collection of articles in memory of Professor Deborah Zamble, a leader in the field of nickel biochemistry.

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Section: Atpase Metallotransporters and Metallochaperonesmentioning

confidence: 99%

Section: Atpase Metallotransporters and Metallochaperonesmentioning

confidence: 99%