1o4t

Protein Summary

Gene TM1287 from Thermotoga maritima translates into the NP_229091 protein from the cupin-2 domain family (PF07883).

TM1287 has a double-stranded beta-helix fold (SCOP sunid:51181), where one turn of helix is made by two pairs of antiparallel strands linked with short turns has the appearance of a  beta-sandwich of distinct architecture and jelly-roll topology. TM1287 belongs to RmlC-like cupins superfamily (SCOP sunid:51182), TM1287-like family. Similar structures according to DALI are: TM1459 protein PDB:1vj2 (chain A, Z=16), PDB:1v70 (chain A, Z=15), TM1010 PDB:2f4p (Z=14), TTHA0104 PDB:2dct (Z=14), PDB:2h0v (chain A, Z=12), PDB:1lr5 (chain A, Z=13), PDB:1yhf (chain A, Z=12), PDB:1rc6 (chain A), PDB:2f4p (chain A), PDB:1sef (chain A), PDB:2b8m (chain A), PDB:1x7n (chain A), PDB:1sfn (chain A), PDB:1j3p (chain A), PDB:1gqg (chain A), PDB:1sq4 (chain A), PDB:1fi2 (chain A), PDB:2fqp (chain A), and PDB:1j58 (chain A). 

1o4t structure was crystallized in the presence of oxalate and manganese. This hypothetical oxalate decarboxylase reveals a bidentate oxalate coordination to the active site manganese ion that in turn chelates residues H61, H63, E68 and H102 (PubMed:15211523). Oxalate decarboxylases regulate oxalate levels in plants and microbes by a Mn²⁺/O₂-dependent carbon-carbon bond cleavage that results in the conversion of oxalate to CO₂ and formate.

Ligand Summary

References