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Literature summary for 2.8.1.7 extracted from

  • Liu, L.; Jiang, S.; Xing, M.; Chen, C.; Lai, C.; Li, N.; Liu, G.; Wu, D.; Gao, H.; Hong, L.; Tan, P.; Chen, S.; Deng, Z.; Wu, G.; Wang, L.
    Structural analysis of an L-cysteine desulfurase from an Ssp DNA phosphorothioation system (2020), mBio, 11, e00488 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.8.1.7

Crystallization (Commentary)

Crystallization (Comment) Organism
structure of mutant C314S in complex with substrate, cysteine, and cofactor, pyridoxal phosphate, at a resolution of 1.80 A. A conformational change is observed in the active site region toward the cysteine substrate to move them close to each other to facilitate the nucleophilic attack Vibrio cyclitrophicus

Protein Variants

Protein Variants Comment Organism
C314S loss of actalytic activity Vibrio cyclitrophicus

Organism

Organism UniProt Comment Textmining
Vibrio cyclitrophicus
-
-
-

Subunits

Subunits Comment Organism
dimer crystallization data Vibrio cyclitrophicus

Synonyms

Synonyms Comment Organism
Sspa
-
 Vibrio cyclitrophicus
stringent starvation protein A
-
 Vibrio cyclitrophicus

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate the cofactor is covalently attached to the side chain amino group of Lys201 in a deep surface pocket via the formation of an internal aldimine Schiff base Vibrio cyclitrophicus

General Information

General Information Comment Organism
physiological function SspA can form a complex with SspD, an ATP diphosphatase Vibrio cyclitrophicus