Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

The asymmetric trimeric architecture of [2Fe-2S] IscU: implications for its scaffolding during iron-sulfur cluster biosynthesis.

Journal of molecular biology - 31 Oct 2008

Shimomura Yoshimitsu, Wada Kei, Fukuyama Keiichi, Takahashi Yasuhiro

Abstract excerpt

IscU is a key component of the ISC machinery and is involved in the biogenesis of iron-sulfur (Fe-S) proteins. IscU serves as a scaffold for assembly of a nascent Fe-S cluster prior to its delivery to an apo protein. Here, we report the first crystal structure of IscU with a bound [2Fe-2S] cluster from the hyperthermophilic bacterium Aquifex aeolicus, determined at a resolution of 2.3 A, using multiwavelength...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acid Substitution
Share to Bacteria

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Crystallography, X-Ray

Share to Iron-Sulfur Proteins

Share to Models, Molecular

Share to Protein Conformation

Share to Protein Structure, Quaternary

Share to Sequence Homology, Amino Acid

Source

Identifiers

PMID: 18723024
DOI: 10.1016/j.jmb.2008.08.015

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The asymmetric trimeric architecture of [2Fe-2S] IscU: implications for its scaffolding during iron-sulfur cluster biosynthesis.PMID 18723024Read ↗

Expression, purification and characterization of an iron-sulfur cluster assembly protein, IscU, from Acidithiobacillus ferrooxidans.Semantic proximity Read ↗

Evidence for dynamic in vivo interconversion of the conformational states of IscU during iron-sulfur cluster biosynthesis.Semantic proximity Read ↗

The IscA from Acidithiobacillus ferrooxidans is an iron-sulfur protein which assemble the [Fe4S4] cluster with intracellular iron and sulfur.Semantic proximity Read ↗

Iron-sulfur cluster biosynthesis: characterization of IscU-IscS complex formation and a structural model for sulfide delivery to the [2Fe-2S] assembly site.Semantic proximity Read ↗

Iron binding activity is essential for the function of IscA in iron-sulphur cluster biogenesis.Semantic proximity Read ↗

Structural properties of [2Fe-2S] ISCA2-IBA57: a complex of the mitochondrial iron-sulfur cluster assembly machinery.Semantic proximity Read ↗

Iron-sulfur-protein biogenesis in eukaryotes.Semantic proximity Read ↗

Novel features of the ISC machinery revealed by characterization of Escherichia coli mutants that survive without iron-sulfur clusters.Semantic proximity Read ↗

The yeast scaffold proteins Isu1p and Isu2p are required inside mitochondria for maturation of cytosolic Fe/S proteins.Semantic proximity Read ↗

A Tetranuclear Cu(I) Cluster in the Metallochaperone Protein CopZSemantic proximity Read ↗

Salmonella enterica requires ApbC function for growth on tricarballylate: evidence of functional redundancy between ApbC and IscU.Semantic proximity Read ↗

Iron-sulfur cluster assembly: NifU-directed activation of the nitrogenase Fe protein.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.