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Literature summary extracted from

  • Zubieta, C.; Krishna, S.S.; McMullan, D.; Miller, M.D.; Abdubek, P.; Agarwalla, S.; Ambing, E.; Astakhova, T.; Axelrod, H.L.; Carlton, D.; Chiu, H.; Clayton, T.; Deller, M.; DiDonato, M.; Duan, L.; Elsliger, M.; Grzechnik, S.K.; Hale, J.; Hampton, E.; Han, G.W.; Haugen, J.; Jaroszewski, L.; Jin, K.K.; Klock, H.E.; Knuth, M.W.; Koesema, E.; Kumar, A.; Marciano, D.; Morse, A.T.; Nigoghossian, E.; Oommachen, S.; Reyes, R.; Rife, C.L.; van den Bedem, H.; Weekes, D.; White, A.; Xu, Q.; Hodgson, K.O.; Wooley, J.; Deacon, A.M.; Godzik, A.; Lesley, S.A.; Wilson, I.A.
    Crystal structure of homoserine O-succinyltransferase from Bacillus cereus at 2.4.ANG. resolution (2007), Proteins Struct. Funct. Bioinform., 68, 999-1005.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.1.46 expressed in Escherichia coli Bacillus cereus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.3.1.46 crystal structure of HTS from Bacillus cereus is determined to 2.4 A resolution. HTS is a single-domain protein with a Rossmann fold topology. The core of the protein is a parallel beta-sheet sandwiched by alpha-helices. HTS is composed of 11 beta-strands, 7 alpha-helices, and four 310-helices Bacillus cereus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.3.1.46 70000
-
gel filtration Bacillus cereus

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.46 Bacillus cereus Q72X44
-
-

Subunits

EC Number Subunits Comment Organism
2.3.1.46 dimer
-
Bacillus cereus

Synonyms

EC Number Synonyms Comment Organism
2.3.1.46 homoserine O-succinyltransferase
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Bacillus cereus
2.3.1.46 HTS
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Bacillus cereus