Literature summary for 2.8.1.7 extracted from

Dunkle, J.A.; Bruno, M.R.; Outten, F.W.; Frantom, P.A.
Structural evidence for dimer-interface-driven regulation of the type II cysteine desulfurase, SufS (2019), Biochemistry, 58, 687-696 .

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Crystallization (Commentary)

Crystallization (Comment)	Organism
structure of the SufS homodimer which adopts a state in which the two monomers are rotated relative to their resting state, displacing a beta-hairpin from its typical position blocking transpersulfurase access to the SufS active site. The active-site beta-hairpin is likely to require adjacent structural elements to function as a beta-latch regulating access to the SufS active site	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P77444	-	-

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Release 2023.1 (January 2023)