National Center for
2JH3: The Crystal Structure Of Dr2241 From Deinococcus Radiodurans At 1.9 A Resolution Reveals A Multi-Domain Protein With Structural Similarity To Chelatases But Also With Two Additional Novel Domains
The crystal structure of DR2241 from Deinococcus radiodurans at 1.9 Å resolution reveals a multi-domain protein with structural similarity to chelatases but also with two additional novel domains
J. Struct. Biol. (2007) 159 p.92-102
A unique family of proteins have been identified in the Deinococcus genus with an N-terminal cobalamin (vitamin B(12)) chelatase domain denoted CbiX and an additional unique C-terminal domain with unknown function. Here we report the first crystal structure from this new family of proteins with the structure of Deinococcus radiodurans protein DR2241. The structure reveals a multi-domain protein where domains A (residues 1-132) has the same fold as the small CbiX (CbiX(S)), domains A and B (residues 1-272) follow the chelatase super-family fold and the two additional unique domains C and D have no structural homologues. Domain D harbours the sequence motifs CxxC and CxxxC, in which DR2241 gives the first evidence that these motifs bind a [4Fe-4S] iron-sulphur cluster. In solution there are indications of multimeric forms, and in the crystallographic asymmetric unit a tetramer is found where domains C and D are involved in stabilising the tetrameric assembly.