1U11

PurE (N5-carboxyaminoimidazole Ribonucleotide Mutase) from the acidophile Acetobacter aceti

Summary for 1U11

• Entry DOI: 10.2210/pdb1u11/pdb
• Descriptor: PurE (N5-carboxyaminoimidazole Ribonucleotide Mutase), CITRIC ACID (3 entities in total)
• Functional Keywords: acidophile, pure, protein stability, lyase
• Biological source: Acetobacter aceti
• Total number of polymer chains: 2
• Total formula weight: 37887.28

Authors

Settembre, E.C.,Chittuluru, J.R.,Mill, C.P.,Kappock, T.J.,Ealick, S.E. (deposition date: 2004-07-14, release date: 2004-09-28, Last modification date: 2024-02-14)

Primary citation

Settembre, E.C.,Chittuluru, J.R.,Mill, C.P.,Kappock, T.J.,Ealick, S.E.
Acidophilic adaptations in the structure of Acetobacter aceti N5-carboxyaminoimidazole ribonucleotide mutase (PurE).
Acta Crystallogr.,Sect.D, 60:1753-1760, 2004

PubMed Abstract: 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.

PubMed: 15388921
DOI: 10.1107/S090744490401858X

Experimental method

X-RAY DIFFRACTION (1.55 Å)