Architecture of the yeast mitochondrial iron-sulfur cluster assembly machinery: The sub-complex formed by the iron donor, yfh1 protein, and the scaffold, ISU1 protein

Journal of Biological Chemistry

Volumn 291, Issue 19, 2016, Pages 10378-10398

  Ranatunga, Wasantha ^a   Gakh, Oleksandr ^a   Galeano, Belinda K ^a   Smith, Douglas Y ^a   Söderberg, Christopher A G ^c   Al Karadaghi, Salam ^c   Thompson, James R ^b   Isaya, Grazia ^a  

^a MAYO CLINIC   (United States)

^b MAYO GRADUATE SCHOOL   (United States)

^c LUND UNIVERSITY   (Sweden)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BIOCHEMISTRY; CHEMICAL ANALYSIS; CLUSTER COMPUTING; CROSSLINKING; IRON; IRON COMPOUNDS; MACHINERY; MASS SPECTROMETRY; OLIGOMERS; PROTEINS; SULFUR; YEAST;

CHEMICAL CROSS-LINKING; CYSTEINE DESULFURASE; IRON-SULFUR CLUSTERS; LIMITED PROTEOLYSIS; NEGATIVE STAINING; PROTEIN-PROTEIN INTERACTIONS; SINGLE-PARTICLE ANALYSIS; THREE-DIMENSIONAL RECONSTRUCTION;

SCAFFOLDS (BIOLOGY);

CYSTATHIONINE GAMMA LYASE; FUNGAL PROTEIN; IRON SULFUR PROTEIN; PROTEIN ISU1; PROTEIN NFS1; UNCLASSIFIED DRUG; YEAST FRATAXIN HOMOLOGUE 1; FRATAXIN; IRON; IRON BINDING PROTEIN; ISU1 PROTEIN, S CEREVISIAE; MITOCHONDRIAL PROTEIN; PROTEIN BINDING; SACCHAROMYCES CEREVISIAE PROTEIN; SULFUR;

ARTICLE; COMPLEX FORMATION; CONTROLLED STUDY; CROSS LINKING; MASS SPECTROMETRY; MITOCHONDRION; MOLECULAR DYNAMICS; MOLECULAR INTERACTION; MOLECULAR MODEL; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN ASSEMBLY; PROTEIN BINDING; PROTEIN DEGRADATION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; SACCHAROMYCES CEREVISIAE; STOICHIOMETRY; THREE DIMENSIONAL IMAGING; TRANSMISSION ELECTRON MICROSCOPY; CHEMISTRY; GROWTH, DEVELOPMENT AND AGING; METABOLISM; PROTEIN CONFORMATION; X RAY CRYSTALLOGRAPHY;

CRYSTALLOGRAPHY, X-RAY; IRON; IRON-BINDING PROTEINS; IRON-SULFUR PROTEINS; MITOCHONDRIA; MITOCHONDRIAL PROTEINS; MODELS, MOLECULAR; PROTEIN BINDING; PROTEIN CONFORMATION; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; SULFUR;

EID: 84966319172     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M115.712414     Document Type: Article

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