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Literature summary for 5.4.99.19 extracted from

  • Sivaraman, J.; Sauve, V.; Larocque, R.; Stura, E.A.; Schrag, J.D.; Cygler, M.; Matte, A.
    Structure of the 16S rRNA pseudouridine synthase RsuA bound to uracil and UMP (2002), Nat. Struct. Biol., 9, 353-358.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
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Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
sitting drop vapor diffusion at 18°C, crystal structure of RsuA bound to uracil at 2.0 A resolution and to uridine 5'-monophosphate at 2.65 A resolution. RsuA consists of an N-terminal domain connected by an extended linker to the central and C-terminal domains. Uracil and UMP bind in a cleft between the central and C-terminal domains near the catalytic residue Asp102. The N-terminal domain shows structural similarity to the ribosomal protein S4. Despite only 15% amino acid identity, the other two domains are structurally similar to those of the tRNA-specific Psi-synthase TruA, including the position of the catalytic Asp Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P0AA43
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-

Purification (Commentary)

Purification (Comment) Organism
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Escherichia coli

Synonyms

Synonyms Comment Organism
PSI-synthase RsuA
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Escherichia coli
RsuA
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Escherichia coli