Publication Abstract from PubMed
The crystal structure of Acetobacter aceti PurE was determined to a resolution of 1.55 A and is compared with the known structures of the class I PurEs from a mesophile, Escherichia coli, and a thermophile, Thermotoga maritima. Analyses of the general factors that increase protein stability are examined as potential explanations for the acid stability of A. aceti PurE. Increased inter-subunit hydrogen bonding and an increased number of arginine-containing salt bridges appear to account for the bulk of the increased acid stability. A chain of histidines linking two active sites is discussed in the context of the proton transfers catalyzed by the enzyme.
Acidophilic adaptations in the structure of Acetobacter aceti N5-carboxyaminoimidazole ribonucleotide mutase (PurE).,Settembre EC, Chittuluru JR, Mill CP, Kappock TJ, Ealick SE Acta Crystallogr D Biol Crystallogr. 2004 Oct;60(Pt 10):1753-60. Epub 2004, Sep 23. PMID:15388921[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
