2E69

Crystal structure of the stationary phase survival protein SurE from Thermus thermophilus HB8 in complex with sulfate

Summary for 2E69

• Entry DOI: 10.2210/pdb2e69/pdb
• Related: 1ILV 1J9J 1J9K 1J9L 1L5X 2E6B 2E6C 2E6E 2E6G 2E6H
• Descriptor: 5'-nucleotidase surE, SULFATE ION, GLYCEROL, ... (4 entities in total)
• Functional Keywords: sure protein, hydrolase
• Biological source: Thermus thermophilus
• Cellular location: Cytoplasm (Potential): Q53W92
• Total number of polymer chains: 4
• Total formula weight: 108030.22

Authors

Iwasaki, W.,Miki, K. (deposition date: 2006-12-26, release date: 2007-08-28, Last modification date: 2023-10-25)

Primary citation

Iwasaki, W.,Miki, K.
Crystal Structure of the Stationary Phase Survival Protein SurE with Metal Ion and AMP
J.Mol.Biol., 371:123-136, 2007

PubMed Abstract: The stationary phase survival protein SurE is a metal ion-dependent phosphatase distributed among eubacteria, archaea, and eukaryotes. In Escherichia coli, SurE has activities as nucleotidase and exopolyphosphatase, and is thought to be involved in stress response. However, its physiological role and reaction mechanism are unclear. We report here the crystal structures of the tetramer of SurE from Thermus thermophilus HB8 (TtSurE) both alone and crystallized with Mn(2+) and substrate AMP. In the presence of Mn(2+) and AMP, differences between the protomers were observed in the active site and in the loop located near the active site; AMP-bound active sites with the loops in a novel open conformation were found in the two protomers, and AMP-free active sites with the loops in a conventional closed conformation were found in the other two protomers. The two loops in the open conformation are entwined with each other, and this entwining is suggested to be required for enzymatic activity by site-directed mutagenesis. TtSurE exists as an equilibrium mixture of dimer and tetramer in solution. The loop-entwined structure indicates that SurE acts as a tetramer. The structural features and the absence of negative cooperativity imply the half-of-the-sites reactivity mechanism resulting from a pre-existing tendency toward structural asymmetry.

PubMed: 17561111
DOI: 10.1016/j.jmb.2007.05.007

Experimental method

X-RAY DIFFRACTION (2.2 Å)