2MJD

Oxidized Yeast Adrenodoxin Homolog 1

Summary for 2MJD

• Entry DOI: 10.2210/pdb2mjd/pdb
• Related: 2MJE
• NMR Information: BMRB: 19717
• Descriptor: Adrenodoxin homolog, mitochondrial, FE2/S2 (INORGANIC) CLUSTER (2 entities in total)
• Functional Keywords: ferredoxin, iron sulfur assembly, paramagnetic protein, 2fe2s cluster, metal binding protein
• Biological source: Saccharomyces cerevisiae (Baker's yeast)
• Cellular location: Mitochondrion matrix : Q12184
• Total number of polymer chains: 1
• Total formula weight: 12810.83

Authors

Gallo, A.,Banci, L. (deposition date: 2014-01-07, release date: 2014-11-19, Last modification date: 2024-05-15)

Primary citation

Webert, H.,Freibert, S.A.,Gallo, A.,Heidenreich, T.,Linne, U.,Amlacher, S.,Hurt, E.,Muhlenhoff, U.,Banci, L.,Lill, R.
Functional reconstitution of mitochondrial Fe/S cluster synthesis on Isu1 reveals the involvement of ferredoxin.
Nat Commun, 5:5013-5013, 2014

PubMed Abstract: Maturation of iron-sulphur (Fe/S) proteins involves complex biosynthetic machinery. In vivo synthesis of [2Fe-2S] clusters on the mitochondrial scaffold protein Isu1 requires the cysteine desulphurase complex Nfs1-Isd11, frataxin, ferredoxin Yah1 and its reductase Arh1. The roles of Yah1-Arh1 have remained enigmatic, because they are not required for in vitro Fe/S cluster assembly. Here, we reconstitute [2Fe-2S] cluster synthesis on Isu1 in a reaction depending on Nfs1-Isd11, frataxin, Yah1, Arh1 and NADPH. Unlike in the bacterial system, frataxin is an essential part of Fe/S cluster biosynthesis and is required simultaneously and stoichiometrically to Yah1. Reduced but not oxidized Yah1 tightly interacts with apo-Isu1 indicating a dynamic interaction between Yah1-apo-Isu1. Nuclear magnetic resonance structural studies identify the Yah1-apo-Isu1 interaction surface and suggest a pathway for electron flow from reduced ferredoxin to Isu1. Together, our study defines the molecular function of the ferredoxin Yah1 and its human orthologue FDX2 in mitochondrial Fe/S cluster synthesis.

PubMed: 25358379
DOI: 10.1038/ncomms6013

Experimental method

SOLUTION NMR