Pub. Date : 2019 Oct 21
PMID : 31273981
14 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Bimodal Nickel-Binding Site on Escherichia coli [NiFe]-Hydrogenase Metallochaperone HypA. | Nickel | hypA | Escherichia coli |
| 2 | The penultimate maturation step is the delivery of nickel to a primed hydrogenase enzyme precursor protein, a process that is accomplished by two nickel metallochaperones, the accessory protein HypA and the GTPase HypB. | Nickel | hypA | Escherichia coli |
| 3 | The penultimate maturation step is the delivery of nickel to a primed hydrogenase enzyme precursor protein, a process that is accomplished by two nickel metallochaperones, the accessory protein HypA and the GTPase HypB. | Nickel | hypA | Escherichia coli |
| 4 | Recent work demonstrated that nickel is rapidly transferred to HypA from GDP-loaded HypB within the context of a protein complex in a nickel selective and unidirectional process. | Nickel | hypA | Escherichia coli |
| 5 | Recent work demonstrated that nickel is rapidly transferred to HypA from GDP-loaded HypB within the context of a protein complex in a nickel selective and unidirectional process. | Nickel | hypA | Escherichia coli |
| 6 | To investigate the mechanism of metal transfer, we examined the allosteric effects of nucleotide cofactors and partner proteins on the nickel environments of HypA and HypB by using a combination of biochemical, microbiological, computational, and spectroscopic techniques. | Nickel | hypA | Escherichia coli |
| 7 | In addition, interaction with a mutant version of HypA with disrupted nickel binding, H2Q-HypA, does not induce substantial changes to the HypB G-domain nickel site. | Nickel | hypA | Escherichia coli |
| 8 | In addition, interaction with a mutant version of HypA with disrupted nickel binding, H2Q-HypA, does not induce substantial changes to the HypB G-domain nickel site. | Nickel | hypA | Escherichia coli |
| 9 | Analysis of a peptide maquette derived from the N-terminus of HypA revealed that nickel is predominately coordinated by atoms from the N-terminal Met-His motif. | Nickel | hypA | Escherichia coli |
| 10 | Furthermore, HypA is capable of two nickel-binding modes at the N-terminus, a HypB-induced mode and a binding mode that mirrors the peptide maquette. | Nickel | hypA | Escherichia coli |
| 11 | Collectively, these results reveal that HypB brings about changes in the nickel coordination of HypA, providing a mechanism for the HypB-dependent control of the acquisition and release of nickel by HypA. | Nickel | hypA | Escherichia coli |
| 12 | Collectively, these results reveal that HypB brings about changes in the nickel coordination of HypA, providing a mechanism for the HypB-dependent control of the acquisition and release of nickel by HypA. | Nickel | hypA | Escherichia coli |
| 13 | Collectively, these results reveal that HypB brings about changes in the nickel coordination of HypA, providing a mechanism for the HypB-dependent control of the acquisition and release of nickel by HypA. | Nickel | hypA | Escherichia coli |
| 14 | Collectively, these results reveal that HypB brings about changes in the nickel coordination of HypA, providing a mechanism for the HypB-dependent control of the acquisition and release of nickel by HypA. | Nickel | hypA | Escherichia coli |