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Literature summary for 2.5.1.49 extracted from

  • Tran, T.H.; Krishnamoorthy, K.; Begley, T.P.; Ealick, S.E.
    A novel mechanism of sulfur transfer catalyzed by O-acetylhomoserine sulfhydrylase in the methionine-biosynthetic pathway of Wolinella succinogenes (2011), Acta Crystallogr. Sect. D, 67, 831-838.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
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Wolinella succinogenes

Crystallization (Commentary)

Crystallization (Comment) Organism
to 2.2 A resolution, space group C2, two monomers per asymmetric unit. The monomer adopts an alpha/beta fold and consists of a large central seven-stranded beta-sheet, a two-stranded beta-sheet and a three-stranded beta-sheet. The beta-sheets are flanked by a total of 12 alpha-helices and two 3(10)-helices. The active site is located near the N-terminus of alpha3. The pydridoxal 5'-phosphate-binding site is occupied by water molecules in the absence of the cofactor. The phosphate group of pydridoxal 5'-phosphate makes hydrogen bonds to Thr204, Ser202 and the amide N-atoms of Gly83 and Met84. Asp180 is within salt-bridge distance of the N1 atom of pydridoxal 5'-phosphate. Leu353, Met183, Ile87 and Met84 interact with the hydrophobic region of pydridoxal 5'-phosphate Wolinella succinogenes

Organism

Organism UniProt Comment Textmining
Wolinella succinogenes Q7M844
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Synonyms

Synonyms Comment Organism
MetY
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Wolinella succinogenes
OAHS
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Wolinella succinogenes

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate
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Wolinella succinogenes