Literature summary for 1.8.99.5 extracted from

Schiffer, A.; Parey, K.; Warkentin, E.; Diederichs, K.; Huber, H.; Stetter, K.O.; Kroneck, P.M.; Ermler, U.
Structure of the dissimilatory sulfite reductase from the hyperthermophilic archaeon Archaeoglobus fulgidus (2008), J. Mol. Biol., 379, 1063-1074.

Cloned(Commentary)

Cloned (Comment)	Organism
-	Archaeoglobus fulgidus

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystal structure at 2 A resolution and comparison with that of the phylogenetically related assimilatory sulfite reductase aSir. Dissimilatory sulfite reductase dSir is organized as a heterotetrameric complex composed of two catalytically independent alphabeta heterodimers. aSir is a monomeric protein built of two fused modules. aSir binds one siroheme-[4Fe-4S] center, dSir harbors two of them within each alphabeta heterodimer. Only one siroheme-[4Fe-4S] center in each alphabeta heterodimer is catalytically active, whereas access to the second one is blocked by a tryptophan residue	Archaeoglobus fulgidus

Crystallization (Comment)

Organism

crystal structure at 2 A resolution and comparison with that of the phylogenetically related assimilatory sulfite reductase aSir. Dissimilatory sulfite reductase dSir is organized as a heterotetrameric complex composed of two catalytically independent alphabeta heterodimers. aSir is a monomeric protein built of two fused modules. aSir binds one siroheme-[4Fe-4S] center, dSir harbors two of them within each alphabeta heterodimer. Only one siroheme-[4Fe-4S] center in each alphabeta heterodimer is catalytically active, whereas access to the second one is blocked by a tryptophan residue

Archaeoglobus fulgidus

Organism

Organism	UniProt	Comment	Textmining
Archaeoglobus fulgidus	Q59109 and Q59110	Q59109 i.e. subunit DsrA, Q59110 i.e. subunit DsrB	-

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Release 2023.1 (January 2023)