Publication Date:
2016-02-24
Description:
Crystal structures of 5-aminoimidazole ribonucleotide (AIR) synthetase, also known as PurM, from Thermus thermophilus ( Tt ) and Geobacillus kaustophilus ( Gk ) were determined. For Tt PurM, the maximum resolution was 2.2 Å and the space group was P 2 1 2 1 2 with four dimers in an asymmetric unit. For Gk PurM, the maximum resolution was 2.2 Å and the space group was P 2 1 2 1 2 with one monomer in asymmetric unit. The biological unit is dimer for both Tt PurM and Gk PurM and the dimer structures were similar to previously determined structures of PurM in general. For Tt PurM, ~50 residues at the amino terminal were disordered in the crystal structure whereas, for Gk PurM, the corresponding region covered the ATP-binding site forming an α helix in part, suggesting that the N-terminal region of PurM changes its conformation upon binding of ligands. FGAM binding site was predicted by the docking simulation followed by the MD simulation based on the SO 4 2– binding site found in the crystal structure of Tt PurM.
Print ISSN:
0021-924X
Electronic ISSN:
1756-2651
Topics:
Biology
,
Chemistry and Pharmacology