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6.3.5.6: asparaginyl-tRNA synthase (glutamine-hydrolysing)

This is an abbreviated version!
For detailed information about asparaginyl-tRNA synthase (glutamine-hydrolysing), go to the full flat file.

Word Map on EC 6.3.5.6

Reaction

4-phosphooxy-L-aspartyl-tRNAAsn
+
NH3
=
L-asparaginyl-tRNAAsn
 +
phosphate

Synonyms

AdT, AsnRS, Asp-AdT, Asp-tRNAAsn amidotransferase, Asp/Glu-Adt, asparaginyl-transfer RNA synthetase, Asparaginyl-tRNA synthetase, aspartyl-tRNAAsn amidotransferase, GatCAB, glutamine-dependent Asp-tRNAAsn/Glu-tRNAGln amidotransferase, NRS, tRNA-dependent amidotransferase

ECTree

     6 Ligases
         6.3 Forming carbon-nitrogen bonds
             6.3.5 Carbon-nitrogen ligases with glutamine as amido-N-donor
                6.3.5.6 asparaginyl-tRNA synthase (glutamine-hydrolysing)

Crystallization

Crystallization on EC 6.3.5.6 - asparaginyl-tRNA synthase (glutamine-hydrolysing)

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structures of the catalytically active N-terminally truncated enzyme (residues 112-548) is solved by X-ray crystallography. The N-terminal domain contains a structured region with a novel fold featuring a lysine-rich helix that is shown by NMR to interact with tRNA. This is connected by an unstructured tether to the remainder of the enzyme, which is highly similar to the known structure of bacterial AsnRS