ArticleProceedings of the National Academy of Sciences of the United States of America2015
Structural basis of a Ni acquisition cycle for [NiFe] hydrogenase by Ni-metallochaperone HypA and its enhancer.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 58 citations in OpenAlex.
- The HypA and HypB metallochaperones from Methanococcus maripaludis have unique metal-binding properties and a distinct nickel transfer mechanism.The Journal of biological chemistry · 2026Article
- Biosynthesis and assembly of hydrogenase [NiFe]-cofactor: recent advances and perspectives.Metallomics : integrated biometal science · 2025Review
- A metal-trap tests and refines blueprints to engineer cellular protein metalation with different elements.Nature communications · 2025Article
- Stepwise assembly of the active site of [NiFe]-hydrogenase.Nature chemical biology · 2023Article
- Protein metalation in a nutshell.FEBS letters · 2023Review
- Basaltic Lava Tube Hosts a Putative Novel Genus in the FamilyMicrobiology resource announcements · 2022Article
- The role of nucleoside triphosphate hydrolase metallochaperones in making metalloenzymes.Metallomics : integrated biometal science · 2022Review
- Electron inventory of the iron-sulfur scaffold complex HypCD essential in [NiFe]-hydrogenase cofactor assembly.The Biochemical journal · 2021Article
- The requirement for cobalt in vitamin BBiochimica et biophysica acta. Molecular cell research · 2021Review
- A membrane-bound [NiFe]-hydrogenase large subunit precursor whose C-terminal extension is not essential for cofactor incorporation but guarantees optimal maturation.MicrobiologyOpen · 2020Article
- An overview of 25 years of research on Thermococcus kodakarensis, a genetically versatile model organism for archaeal research.Folia microbiologica · 2020Review
- Bimodal Nickel-Binding Site onInorganic chemistry · 2019Article
- The Metallochaperone Encoding GeneMicroorganisms · 2019Article
- Nickel Metalloregulators and Chaperones.Inorganics · 2019Article
- Structure and dynamics of Helicobacter pylori nickel-chaperone HypA: an integrated approach using NMR spectroscopy, functional assays and computational tools.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018Article
- Crystal structures of a [NiFe] hydrogenase large subunit HyhL in an immature state in complex with a Ni chaperone HypA.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- In-vivo turnover frequency of the cyanobacterial NiFe-hydrogenase during photohydrogen production outperforms in-vitro systems.Scientific reports · 2018Article
- Structural and Phylogenetic Diversity of Anaerobic Carbon-Monoxide Dehydrogenases.Frontiers in microbiology · 2018Article
- Proteolytic cleavage orchestrates cofactor insertion and protein assembly in [NiFe]-hydrogenase biosynthesis.The Journal of biological chemistry · 2017Article
- Mycobacterium tuberculosis proteasomal ATPase Mpa has a β-grasp domain that hinders docking with the proteasome core protease.Molecular microbiology · 2017Article
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Ni atom at the catalytic center of [NiFe] hydrogenases is incorporated by a Ni-metallochaperone, HypA, and a GTPase/ATPase, HypB. We report the crystal structures of the transient complex formed between HypA and ATPase-type HypB (HypBAT) with Ni ions. Transient association between HypA and HypBAT is controlled by the ATP hydrolysis cycle of HypBAT, which is accelerated by HypA. Only the ATP-bound form of HypBAT can interact with HypA and induces drastic conformational changes of HypA. Consequently, upon complex formation, a conserved His residue of HypA comes close to the N-terminal conserved motif of HypA and forms a Ni-binding site, to which a Ni ion is bound with a nearly square-planar geometry. The Ni binding site in the HypABAT complex has a nanomolar affinity (Kd = 7 nM), which is in contrast to the micromolar affinity (Kd = 4 µM) observed with the isolated HypA. The ATP hydrolysis and Ni binding cause conformational changes of HypBAT, affecting its association with HypA. These findings indicate that HypA and HypBAT constitute an ATP-dependent Ni acquisition cycle for [NiFe]-hydrogenase maturation, wherein HypBAT functions as a metallochaperone enhancer and considerably increases the Ni-binding affinity of HypA.
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