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2.1.2.13: UDP-4-amino-4-deoxy-L-arabinose formyltransferase

This is an abbreviated version!
For detailed information about UDP-4-amino-4-deoxy-L-arabinose formyltransferase, go to the full flat file.

Reaction

10-formyltetrahydrofolate
+
UDP-4-amino-4-deoxy-beta-L-arabinopyranose
=
5,6,7,8-tetrahydrofolate
+
UDP-4-deoxy-4-formamido-beta-L-arabinopyranose

Synonyms

ArnA, ArnA formyltransferase, ArnAFT, Pmrl

ECTree

     2 Transferases
         2.1 Transferring one-carbon groups
             2.1.2 Hydroxymethyl-, formyl- and related transferases
                2.1.2.13 UDP-4-amino-4-deoxy-L-arabinose formyltransferase

Crystallization

Crystallization on EC 2.1.2.13 - UDP-4-amino-4-deoxy-L-arabinose formyltransferase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallization of native and Se-Met decarboxylase protein. Good quality crystals are obtained with a precipitant solution of 3.2 M NaCl, 0.1 M Bistris, pH 5.2, using a drop containing 0.004 ml of protein and 0.004 ml of precipitant equilibrated against a reservoir of 0.1 ml of precipitant. Space group as P4(1)3(2), with cell dimensions a = b = c = 149.4 A, beta = gamma = 90°
hanging drop vapor diffusion method, crystal structure of the ArnA transformylase domain is solved to 1.7 A resolution
hanging drop vapor diffusion method, crystal structure of the full-length bifunctional ArnA with UDP-glucuronic acid and ATP bound to the dehydrogenase domain. Binding of UDP-glucuronic acid triggers a 17 A conformational change in ArnA_DH that opens the NAD+ binding site while trapping UDP-glucuronic acid
N-formyltransferase domain of the enzyme in complex with N5-formyltetrahydrofolate and UDP-4-amino-4-deoxy-beta-L-arabinopyranose, hanging drop vapor diffusion method, using 20-22% poly(ethyleneglycol) 5000, 50 mM MgCl2, 100 mM HEPES (pH 8.0) at 21°C
F4SGI5
structure of apo-ArnA and comparison with its ATP- and UDP-glucuronic acid-bound counterparts. In the crystal structure, a binding pocket at the centre of each ArnA trimer in its apo state pocket is occupied by a dithiothreitol molecule. Formation of the pocket is linked to a cascade of structural rearrangements that emerge from the NAD+-binding site. A small effector molecule is postulated that binds to the central pocket and modulates the catalytic properties of ArnA