Structural highlights
Function
[Q2QJL3_ACEAC] Catalyzes the conversion of N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole ribonucleotide (CAIR) (By similarity).[PIRNR:PIRNR001338]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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.
See Also
References
- ↑ Settembre EC, Chittuluru JR, Mill CP, Kappock TJ, Ealick SE. Acidophilic adaptations in the structure of Acetobacter aceti N5-carboxyaminoimidazole ribonucleotide mutase (PurE). Acta Crystallogr D Biol Crystallogr. 2004 Oct;60(Pt 10):1753-60. Epub 2004, Sep 23. PMID:15388921 doi:10.1107/S090744490401858X
