Open AccessCrystallization and preliminary X‐ray analysis of mannosyl‐3‐phosphoglycerate synthase from Thermus thermophilus HB27
Author(s) -
Gonçalves Susana,
Borges Nuno,
Santos Helena,
Matias Pedro M.
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109032576
Subject(s) - thermus thermophilus , thermophile , crystallization , crystallography , dimer , chemistry , atp synthase , monoclinic crystal system , crystal structure , biochemistry , enzyme , escherichia coli , organic chemistry , gene
Mannosylglycerate (MG) is a compatible solute that is widespread in marine organisms that are adapted to hot environments, with its intracellular pool generally increasing in response to osmotic stress. These observations suggest that MG plays a relevant role in osmoadaptation and thermoadaptation. The pathways for the synthesis of MG have been characterized in a number of thermophilic and hyperthermophilic organisms. Mannosyl‐3‐phosphoglycerate synthase (MpgS) is a key enzyme in the biosynthesis of MG. Here, the purification, crystallization and preliminary crystallographic characterization of apo MpgS from Thermus thermophilus HB27 are reported. The addition of Zn 2+ to the crystallization buffer was essential in order to obtain crystals. The crystals belonged to one of the enantiomorphic tetragonal space groups P 4 1 2 1 2 or P 4 3 2 1 2, with unit‐cell parameters a = b = 113, c = 197 Å. Diffraction data were obtained to a resolution of 2.97 Å.