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Structure paper

TitleThe external aldimine form of mutant beta-S377A Salmonella thypi tryptophan synthase in open conformation showing dual side chain conformations for the residue beta-Q114, sodium ion at the metal coordination site, and F9 inhibitor at the alpha-site. One of the beta-Q114 rotamer conformations allows a hydrogen bond to form with the PLP oxygen at the position 3 in the ring.
Journal, issue, pagesTo be Published
Publish dateAug 2, 2020 (structure data deposition date)
AuthorsHilario, E. / Dunn, M.F. / Mueller, L.J.
External linksSearch PubMed
MethodsX-ray diffraction
Resolution1.6 Å
Structure data

PDB-7jmq:
The external aldimine form of the mutant beta-S377A Salmonella thypi tryptophan synthase in open conformation showing dual side chain conformations for the residue beta-Q114, sodium ion at the metal coordination site, and F9 inhibitor at the alpha-site. One of the beta-Q114 rotamer conformations allows a hydrogen bond to form with the PLP oxygen at the position 3 in the ring
Method: X-RAY DIFFRACTION / Resolution: 1.6 Å

Chemicals

ChemComp-DMS:
DIMETHYL SULFOXIDE / DMSO, precipitant*YM

ChemComp-F9F:
2-({[4-(TRIFLUOROMETHOXY)PHENYL]SULFONYL}AMINO)ETHYL DIHYDROGEN PHOSPHATE

ChemComp-CS:
Unknown entry

ChemComp-KOU:
(E)-N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-L-serine

ChemComp-GOL:
GLYCEROL

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-NA:
Unknown entry

ChemComp-CL:
Unknown entry

ChemComp-HOH:
WATER

Source
  • salmonella typhimurium (strain lt2 / sgsc1412 / atcc 700720) (bacteria)
KeywordsLYASE / protein complex / F9F / internal aldimine

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