Literature summary for 3.1.11.6 extracted from

Poleszak, K.; Kaminska, K.H.; Dunin-Horkawicz, S.; Lupas, A.; Skowronek, K.J.; Bujnicki, J.M.
Delineation of structural domains and identification of functionally important residues in DNA repair enzyme exonuclease VII (2012), Nucleic Acids Res., 40, 8163-8174.

Crystallization (Commentary)

Crystallization (Comment)	Organism
structural analysis using bioinformatics. Large subunit XseA consists of four domains: an N-terminal OB-fold domain, a middle putatively catalytic domain, a coiled-coil domain and a short C-terminal segment. The OB-fold domain is responsible for DNA binding, the coiled-coil domain is involved in binding multiple copies of the XseB subunit and residues D155, R205, H238 and D241 of the middle domain are important for the catalytic activity but not for DNA binding	Escherichia coli

Crystallization (Comment)

Organism

structural analysis using bioinformatics. Large subunit XseA consists of four domains: an N-terminal OB-fold domain, a middle putatively catalytic domain, a coiled-coil domain and a short C-terminal segment. The OB-fold domain is responsible for DNA binding, the coiled-coil domain is involved in binding multiple copies of the XseB subunit and residues D155, R205, H238 and D241 of the middle domain are important for the catalytic activity but not for DNA binding

Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
D155A	mutant of large subunit XseA, complete loss of catalytic activity	Escherichia coli
D241A	mutant of large subunit XseA, complete loss of catalytic activity	Escherichia coli
DELTA397-456	deletion mutant of large subunit XseA, complete loss of catalytic activity	Escherichia coli
F63A	mutant of large subunit XseA, decrease in DNA-binding activity	Escherichia coli
H238A	mutant of large subunit XseA, complete loss of catalytic activity	Escherichia coli
additional information	construction of a series of subunit XseA deletion variants that lack one or several of the helices. Variants with a single helix deleted bind about 70% and variants with two helices deleted about 50% of the subunit XseB levels compared to the full-length XseA. All these deletion variants exhibit a complete loss of exonucleolytic activity in vitro	Escherichia coli
Q96A	mutant of large subunit XseA, shows only mild effects	Escherichia coli
R205A	mutant of large subunit XseA, complete loss of catalytic activity	Escherichia coli
R64E/R68E/R69E	mutant of large subunit XseA, decrease in DNA-binding activity	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Synonyms

Synonyms	Comment	Organism
XseA	large subunit of exonuclease VII	Escherichia coli