Literature summary for 1.21.99.3 extracted from

Schweizer, U.; Schlicker, C.; Braun, D.; K�hrle, J.; Steegborn, C.
Crystal structure of mammalian selenocysteine-dependent iodothyronine deiodinase suggests a peroxiredoxin-like catalytic mechanism (2014), Proc. Natl. Acad. Sci. USA, 111, 10526-10531.

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Cloned(Commentary)

Cloned (Comment)	Organism
-	Mus musculus

Crystallization (Commentary)

Crystallization (Comment)	Organism
structure of the catalytic domain of mouse deiodinase Dio3, to 1.9 A resolution. The catalytic Sec170 is positioned in the loop connecting beta1 to alpha1. It points toward an elongated cleft that likely represents the iodothyronine binding site. The deiodination step follows a selenolate inline attack on the iodine delta-hole weakening the carbon-iodine bond. The abstracted iodonium is replaced by a proton approaching from the opposite side of the ring. The proton is conveyed to the 5-position of the iodothyronine along a triad His219, Glu200, and Ser167, with residues Tyr197 and Thr169 participating in the organization of an intricate H-bond network	Mus musculus

Crystallization (Comment)

Organism

structure of the catalytic domain of mouse deiodinase Dio3, to 1.9 A resolution. The catalytic Sec170 is positioned in the loop connecting beta1 to alpha1. It points toward an elongated cleft that likely represents the iodothyronine binding site. The deiodination step follows a selenolate inline attack on the iodine delta-hole weakening the carbon-iodine bond. The abstracted iodonium is replaced by a proton approaching from the opposite side of the ring. The proton is conveyed to the 5-position of the iodothyronine along a triad His219, Glu200, and Ser167, with residues Tyr197 and Thr169 participating in the organization of an intricate H-bond network

Mus musculus

Protein Variants

Protein Variants	Comment	Organism
E200T	inactive	Mus musculus
S167A	about 10% residual activity	Mus musculus
Sec170C	mutation in active site, crystallization data	Mus musculus
T169A	inactive	Mus musculus
T169S	60% of wild-type activity	Mus musculus
Y197F	inactive	Mus musculus

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
37000	-	2 * 37000, epitope-tagged recombinant protein,SDS-PAGE	Mus musculus
50000	55000	FLAG-tagged recombinant protein, PAGE	Mus musculus

Organism

Organism	UniProt	Comment	Textmining
Mus musculus	Q91ZI8	-	-

Subunits

Subunits	Comment	Organism
dimer	2 * 37000, epitope-tagged recombinant protein,SDS-PAGE	Mus musculus

Synonyms

Synonyms	Comment	Organism
Dio3	-	Mus musculus