Literature summary for 1.7.2.1 extracted from

Tsuda, A.; Ishikawa, R.; Koteishi, H.; Tange, K.; Fukuda, Y.; Kobayashi, K.; Inoue, T.; Nojiri, M.
Structural and mechanistic insights into the electron flow through protein for cytochrome c-tethering copper nitrite reductase (2013), J. Biochem., 154, 51-60.

Crystallization (Commentary)

Crystallization (Comment)	Organism
to 1.95 A resolution. The naturally fused type of Cu-nitrite reductase tethering a cytochrome c at the C-terminus folds as a unique trimeric domain-swapped structure and has a self-sufficient electron flow system. The C-terminal cytochrome c domain is located at the surface of the type 1 copper site in the N-terminal domain from the adjacent subunit. The heme-to-Cu distance of 10.6 A is comparable to the transient electron transfer complex of normal Cu-nitrite reductase with cytochrome c. The cytochrome c-Cu-nitrite reductase domain interaction is highly transient. An electron is directly transferred from the partner to the type 1 copper	Pseudoalteromonas haloplanktis

Crystallization (Comment)

Organism

to 1.95 A resolution. The naturally fused type of Cu-nitrite reductase tethering a cytochrome c at the C-terminus folds as a unique trimeric domain-swapped structure and has a self-sufficient electron flow system. The C-terminal cytochrome c domain is located at the surface of the type 1 copper site in the N-terminal domain from the adjacent subunit. The heme-to-Cu distance of 10.6 A is comparable to the transient electron transfer complex of normal Cu-nitrite reductase with cytochrome c. The cytochrome c-Cu-nitrite reductase domain interaction is highly transient. An electron is directly transferred from the partner to the type 1 copper

Pseudoalteromonas haloplanktis

Metals/Ions

Metals/Ions	Comment	Organism	Structure
copper	the C-terminal cytochrome c domain is located at the surface of the type 1 copper site in the N-terminal domain from the adjacent subunit. The heme-to-Cu distance of 10.6 A is comparable to the transient electron transfer complex of normal Cu-nitrite reductase with cytochrome c	Pseudoalteromonas haloplanktis

Organism

Organism	UniProt	Comment	Textmining
Pseudoalteromonas haloplanktis	-	-	-
Pseudoalteromonas haloplanktis TAC 125	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Pseudoalteromonas haloplanktis

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Release 2023.1 (January 2023)