Literature summary for 1.18.1.5 extracted from

Smith, N.; Mayhew, M.; Holden, M.; Kelly, H.; Robinson, H.; Heroux, A.; Vilker, V.; Gallagher, D.
Structure of C73G putidaredoxin from Pseudomonas putida (2004), Acta Crystallogr. Sect. D, 60, 816-822.

Cloned(Commentary)

Cloned (Comment)	Organism
-	Pseudomonas putida

Crystallization (Commentary)

Crystallization (Comment)	Organism
mutant C73G, to 1.9 A resolution. The C2 crystal contains three putidaredoxin molecules in the asymmetric unit. Findings show a unanimous structure in some regions crucial for electron-transfer interactions, including the cluster-binding loop 39-48 and the cytochrome-interaction region of Asp38 and Trp106. In addition, the Cys45 amide group donates a hydrogen bond to cluster sulfur S1, with Ala46 adopting an Lalpha conformation	Pseudomonas putida

Crystallization (Comment)

Organism

mutant C73G, to 1.9 A resolution. The C2 crystal contains three putidaredoxin molecules in the asymmetric unit. Findings show a unanimous structure in some regions crucial for electron-transfer interactions, including the cluster-binding loop 39-48 and the cytochrome-interaction region of Asp38 and Trp106. In addition, the Cys45 amide group donates a hydrogen bond to cluster sulfur S1, with Ala46 adopting an Lalpha conformation

Pseudomonas putida

Protein Variants

Protein Variants	Comment	Organism
C73G	surface mutation facilitating crystallization without affecting cluster ligation and with only minor effects on activity	Pseudomonas putida

Organism

Organism	UniProt	Comment	Textmining
Pseudomonas putida	-	-	-

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Release 2023.1 (January 2023)