Succinate dehydrogenase subunit E

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SdhE

Solution NMR structure of protein NMA1147 from Neisseria meningitidis. Northeast structural genomics consortium target mr19

Identifiers

Symbol
SdhE

Pfam
PF03937

InterPro
IPR005631

Available protein structures:

Pfam
structures

PDB
RCSB PDB; PDBe; PDBj

PDBsum
structure summary

In molecular biology, the protein domain named Sdh5 is also named SdhE which stands for succinate dehydrogenase protein E. In the past, it has also been named YgfY and DUF339.[1] Another name for sdhE is succinate dehydrogenase assembly factor 2 (sdhaf2).[2] This protein belongs to a group of highly conserved small proteins found in both eukaryotes and prokaryotes, including NMA1147 from Neisseria meningitidis [3] and YgfY from Escherichia coli.[4] The SdhE protein is found on the mitochondrial membrane is it is important for creating energy via a process named the electron transport chain.[1]

Contents

1 Function
2 Structure
3 Protein interactions
4 Human disease
5 History
6 References

Function[edit]
The function of SDHE has been described as a flavinator of succinate dehydrogenase. SdhE works as a co-factor chaperone that incorporates FAD into SdhA. This results in SdhA flavinylation which is required for the proper function succinate dehydrogenase. More recent scientific studies indicate that SdhE is required by bacteria in order to grow on succinate, using succinate as its only source of carbon and additionally for the function, of succinate dehydrogenase, a vital component of the electron transport chain which produces energy.[1]
Structure[edit]
The structure of these proteins consists of a complex bundle of five alpha-helices, which is composed of an up-down 3-helix bundle plus an orthogonal 2-helix bundle.[4]
Protein interactions[edit]
SdhE interacts with the catalytic subunit of the succinate dehydrogenase (SDH) complex.[5]
Human disease[edit]
The human gene named SDH5, encodes for the SdhE protein. The gene itself is located in the chromosomal position 11q13.1. Loss-of-function mutations result in paraganglioma, a neuroendocrine tumour.[5]
History[edit]
The recent studies which suggest SdhE is required for bacterial flavinylation contradict previous thoughts on SdhE. It was originally proposed that FAD incorporation into bacterial flavoproteins was an autocata