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Literature summary for 6.3.5.13 extracted from

  • Leisico, F.; V Vieira, D.; Figueiredo, T.A.; Silva, M.; Cabrita, E.J.; Sobral, R.G.; Ludovice, A.M.; Trincao, J.; Romao, M.J.; de Lencastre, H.; Santos-Silva, T.
    First insights of peptidoglycan amidation in Gram-positive bacteria - the high-resolution crystal structure of Staphylococcus aureus glutamine amidotransferase GatD (2018), Sci. Rep., 8, 5313 .
    View publication on PubMedView publication on EuropePMC
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Cloned(Commentary)

Cloned (Comment) Organism
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 Staphylococcus aureus

Crystallization (Commentary)

Crystallization (Comment) Organism
structure of subunit GatD, at 1.85 A resolution. A glutamine molecule is found close to the active site funnel, hydrogen-bonded to the conserved residue R128 Staphylococcus aureus

Protein Variants

Protein Variants Comment Organism
C94A subunit GatD mutant, totally inactive for glutamine deamidation Staphylococcus aureus
H189A subunit GatD mutant, totally inactive for glutamine deamidation Staphylococcus aureus
R128A subunit GatD mutant, totally inactive for glutamine deamidation Staphylococcus aureus

Organism

Organism UniProt Comment Textmining
Staphylococcus aureus A0A0H2WZ38 and A0A0H2WZQ7 A0A0H2WZ38 i.e. subunit GatD, A0A0H2WZQ7 i.e. subunit MurT
-
Staphylococcus aureus COL A0A0H2WZ38 and A0A0H2WZQ7 A0A0H2WZ38 i.e. subunit GatD, A0A0H2WZQ7 i.e. subunit MurT
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