Proteomics

Dataset Information

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Human mitochondrial cysteine desulfurase complex


ABSTRACT: Cysteine desulfurase plays central role in mitochondrial iron-sulfur cluster biogenesis not only by providing sulfur through the catalysis of L-cysteine to L-alanine but also by serving as the platform for the assembly of other components of the biosynthetic machinery, including ISCU, frataxin, and ferredoxin. Human mitochondrial cysteine desulfurase complex consists of a homodimer with three components: NFS1, ISD11 and acyl carrier protein (ACP). In this study we used chemical crosslinking coupled with tandem mass spectrometry (XC-MS) to investigate the structures of cysteine desulfurase complexes.

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Kai Cai  

LAB HEAD: John L Markley

PROVIDER: PXD009079 | Pride | 2018-07-11

REPOSITORIES: Pride

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Publications

Architectural Features of Human Mitochondrial Cysteine Desulfurase Complexes from Crosslinking Mass Spectrometry and Small-Angle X-Ray Scattering.

Cai Kai K   Frederick Ronnie O RO   Dashti Hesam H   Markley John L JL  

Structure (London, England : 1993) 20180705 8


Cysteine desulfurase plays a central role in mitochondrial iron-sulfur cluster biogenesis by generating sulfur through the conversion of L-cysteine to L-alanine and by serving as the platform for assembling other components of the biosynthetic machinery, including ISCU, frataxin, and ferredoxin. The human mitochondrial cysteine desulfurase complex consists of two copies each of NFS1, ISD11, and acyl carrier protein. We describe results from chemical crosslinking coupled with tandem mass spectrom  ...[more]

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