Literature summary for 1.8.5.3 extracted from

Schindelin, H.; Kisker, C.; Hilton, J.; Rajagopalan, K.; Rees, D.
Crystal structure of DMSO reductase: Redox-linked changes in molybdopterin coordination (1996), Science, 272, 1615-1621.

Crystallization (Commentary)

Crystallization (Comment)	Organism
oxidized Mo(VI)-form, to 3.5 A resolution. Presence of a monooxo molybdenum cofactor containing two molybdopterin guanine dinucleotides that asymmetrically coordinate the molybdenum through their dithiolene groups. One of the pterins exhibits different coordination modes to the molybdenum between the oxidized and reduced states, whereas the side chain oxygen of Ser147 coordinates the metal in both states	Cereibacter sphaeroides

Crystallization (Comment)

Organism

oxidized Mo(VI)-form, to 3.5 A resolution. Presence of a monooxo molybdenum cofactor containing two molybdopterin guanine dinucleotides that asymmetrically coordinate the molybdenum through their dithiolene groups. One of the pterins exhibits different coordination modes to the molybdenum between the oxidized and reduced states, whereas the side chain oxygen of Ser147 coordinates the metal in both states

Cereibacter sphaeroides

Organism

Organism	UniProt	Comment	Textmining
Cereibacter sphaeroides	-	-	-

Cofactor

Cofactor	Comment	Organism	Structure
bis(molybdopterin guanine dinucleotide)molybdenum cofactor	presence of a monooxo molybdenum cofactor containing two molybdopterin guanine dinucleotides that asymmetrically coordinate the molybdenum through their dithiolene groups. One of the pterins exhibits different coordination modes to the molybdenum between the oxidized and reduced states, whereas the side chain oxygen of Ser147 coordinates the metal in both states	Cereibacter sphaeroides

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Release 2023.1 (January 2023)