Cluster and Fold Stability of E. coli ISC-Type Ferredoxin
Explore this paper's citation graph
Summary
NMR relaxation experiments on the cluster-loaded protein show that, once the cluster is in place, the protein forms a globular and relatively rigid domain, indicating that the presence of the iron-sulfur cluster is the switch between a functional and a non-functional state.
- Type
- article
- Published
- 2013-11-12
- Cited by
- 12
- References
- 50
- Access
- Open access
- OpenAlex
- https://openalex.org/W2079869799
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:140597
Keywords
Ferredoxin, Iron–sulfur cluster, Cluster (spacecraft), Chemistry, Protein folding
References
- NMRPipe: A multidimensional spectral processing system based on UNIX pipes
- Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set.
- Protein identification and analysis tools in the ExPASy server.
- Cloning, sequencing, and overexpression of a [2Fe-2S] ferredoxin gene from Escherichia coli.
- Fe:S cluster ligands are the only cysteines required for nitrogenase Fe-protein activities.
- Bacterial IscU is a well folded and functional single domain protein.
- Mars - robust automatic backbone assignment of proteins
- Complete resonance assignment of the first and second apple domains of MIC4 from Toxoplasma gondii, using a new NMRView-based assignment aid
- Adrenodoxin: the archetype of vertebrate-type [2Fe-2S] cluster ferredoxins.
- Genome3D: a UK collaborative project to annotate genomic sequences with predicted 3D structures based on SCOP and CATH domains
- Structure of a [2Fe–2S] ferredoxin from Rhodobacter capsulatus likely involved in Fe–S cluster biogenesis and conformational changes observed upon reduction
- Crystal structure of Escherichia coli Fdx, an adrenodoxin-type ferredoxin involved in the assembly of iron-sulfur clusters.
- A new electron transport mechanism in mitochondrial steroid hydroxylase systems based on structural changes upon the reduction of adrenodoxin.
- Human Ferredoxin-2 Displays a Unique Conformational Change
- Humans possess two mitochondrial ferredoxins, Fdx1 and Fdx2, with distinct roles in steroidogenesis, heme, and Fe/S cluster biosynthesis
- Formation and properties of [4Fe-4S] clusters on the IscU scaffold protein.
- [2Fe-2S]-Ferredoxin Binds Directly to Cysteine Desulfurase and Supplies an Electron for Iron–Sulfur Cluster Assembly but Is Displaced by the Scaffold Protein or Bacterial Frataxin
- Adrenodoxin—A versatile ferredoxin
- Iron-Sulfur Cluster Assembly
- The role of mitochondria in cellular iron-sulfur protein biogenesis and iron metabolism.
Cited by
- Hybrid Methods in Iron-Sulfur Cluster Biogenesis
- The NMR contribution to protein–protein networking in Fe–S protein maturation
- Generalized View of Protein Folding: In Medio Stat Virtus.
- Redox response of iron-sulfur glutaredoxin GRXS17 activates its holdase activity to protect plants from heat stress
- Probing the interaction of ciprofloxacin and E. coli by electrochemistry, spectroscopy and atomic force microscopy.
- Redox Modification of the Iron-Sulfur Glutaredoxin GRXS17 Activates Holdase Activity and Protects Plants from Heat Stress1[OPEN]
- The Di-Iron Protein YtfE Is a Nitric Oxide-Generating Nitrite Reductase Involved in the Management of Nitrosative Stress
- TusA influences Fe-S cluster assembly and iron homeostasis in E. coli by reducing the translation efficiency of Fur
- New insights into the function and molecular mechanisms of Ferredoxin-NADP+ reductase from Brucella ovis.
- Nar1 binds the cytosolic iron sulfur cluster assembly targeting complex via a bipartite interaction interface
- FeS Cluster Assembly: NIF System in Nitrogen‐Fixing Bacteria
Related papers
- Formation of the iron-sulfur cluster of ferredoxin in isolated chloroplasts.
- Folding properties of iron—sulfur proteins
- Cluster characterization in iron-sulfur proteins by magnetic circular dichroism.
- Iron—sulfur cluster micelle as a ferredoxin model
- Structural investigations of the environment of the iron-sulfur cluster of the 2-iron ferredoxins.
- Anaerobic purification and crystallization to improve the crystal quality: ferredoxin II from Desulfovibrio gigas.
- The structure of a novel electron-transfer ferredoxin from Rhodopseudomonas palustris HaA2 which contains a histidine residue in its iron-sulfur cluster-binding motif.