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Structure-function relationships of the Mycobacterium tuberculosis transcription factor WhiB1. [PDF]

open access: yesPLoS ONE, 2012
BackgroundMembers of the WhiB-like (Wbl) protein family possess iron-sulfur clusters and are implicated in the regulation of developmental processes in Actinomycetes. Mycobacterium tuberculosis possesses seven Wbl proteins.
Laura J Smith   +3 more
doaj   +6 more sources

Structural and biochemical investigations of a HEAT-repeat protein involved in the cytosolic iron-sulfur cluster assembly pathway [PDF]

open access: yesCommunications Biology, 2023
Iron-sulfur clusters are essential for life and defects in their biosynthesis lead to human diseases. The mechanism of cluster assembly and delivery to cytosolic and nuclear client proteins via the cytosolic iron-sulfur cluster assembly (CIA) pathway is ...
Sheena Vasquez   +7 more
doaj   +2 more sources

Structure of a Wbl protein and implications for NO sensing by M. tuberculosis [PDF]

open access: yesNature Communications, 2017
Mycobacterium tuberculosis WhiB1 is a DNA-binding protein with a NO sensitive [4Fe-4S] cluster. Here the authors present the NMR structure of WhiB1 and suggest how loss of the iron-sulfur cluster through nitrosylation affects WhiB1 DNA binding and leads ...
Bassam K. Kudhair   +9 more
doaj   +4 more sources

The iron-sulfur cluster is essential for DNA binding by human DNA polymerase ε [PDF]

open access: yesScientific Reports, 2022
DNA polymerase ε (Polε) is a key enzyme for DNA replication in eukaryotes. Recently it was shown that the catalytic domain of yeast Polε (PolεCD) contains a [4Fe-4S] cluster located at the base of the processivity domain (P-domain) and coordinated by ...
Alisa E. Lisova   +5 more
doaj   +2 more sources

Modulation of MagR magnetic properties via iron–sulfur cluster binding

open access: yesScientific Reports, 2021
Iron–sulfur clusters are essential cofactors found in all kingdoms of life and play essential roles in fundamental processes, including but not limited to respiration, photosynthesis, and nitrogen fixation.
Zhen Guo   +11 more
doaj   +1 more source

Regulation of Mitochondrial Energy Metabolism by Glutaredoxin 5 in the Apicomplexan Parasite Neospora caninum

open access: yesMicrobiology Spectrum, 2023
Iron-sulfur [Fe-S] clusters are one of the most ancient and functionally versatile natural biosynthetic prosthetic groups required by various proteins involved in important metabolic processes, including the oxidative phosphorylation of proteins ...
Xingju Song   +5 more
doaj   +1 more source

Constraint-based modeling of yeast mitochondria reveals the dynamics of protein import and iron-sulfur cluster biogenesis

open access: yesiScience, 2021
Summary: Mitochondria are a hallmark of eukaryal cells and play an important role in cellular metabolism. There is a vast amount of knowledge available on mitochondrial metabolism and essential mitochondrial functions, such as protein import and iron ...
Carl Malina   +3 more
doaj   +1 more source

Structure of a putative immature form of a Rieske-type iron-sulfur protein in complex with zinc chloride

open access: yesCommunications Chemistry, 2023
Iron-sulfur clusters are prosthetic groups of proteins involved in various biological processes. However, details of the immature state of the iron-sulfur cluster into proteins have not yet been elucidated. We report here the first structural analysis of
Erika Tsutsumi   +9 more
doaj   +1 more source

Crystallographic characterization of the high-potential iron-sulfur protein in the oxidized state at 0.8 Å resolution. [PDF]

open access: yesPLoS ONE, 2017
High-potential iron-sulfur protein (HiPIP) is a soluble electron carrier protein of photosynthetic bacteria with an Fe4S4 cluster. Although structural changes accompanying the electron transfer are important for understanding of the functional mechanism,
Hiraku Ohno   +6 more
doaj   +1 more source

Sulfur Administration in Fe–S Cluster Homeostasis

open access: yesAntioxidants, 2021
Mitochondria are the key organelles of Fe–S cluster synthesis. They contain the enzyme cysteine desulfurase, a scaffold protein, iron and electron donors, and specific chaperons all required for the formation of Fe–S clusters.
Leszek Rydz   +2 more
doaj   +1 more source

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