1L5X

The 2.0-Angstrom resolution crystal structure of a survival protein E (SurE) homolog from Pyrobaculum aerophilum

Summary for 1L5X

• Entry DOI: 10.2210/pdb1l5x/pdb
• Related: 1ILV 1J9J 1J9K 1J9L
• Descriptor: Survival protein E, GLYCEROL, ACETIC ACID, ... (4 entities in total)
• Functional Keywords: structural genomics, putative acid phosphatase, mixed alpha/beta protein, n-terminal rossmann-fold like, novel c-terminal domain with beta-hairpin extensions, unknown function
• Biological source: Pyrobaculum aerophilum
• Cellular location: Cytoplasm (Potential): Q8ZU79
• Total number of polymer chains: 2
• Total formula weight: 62301.31

Authors

Mura, C.,Katz, J.E.,Clarke, S.G.,Eisenberg, D. (deposition date: 2002-03-08, release date: 2003-02-25, Last modification date: 2024-10-30)

Primary citation

Mura, C.,Katz, J.E.,Clarke, S.G.,Eisenberg, D.
Structure and Function of an Archaeal Homolog of Survival Protein E (SurE-alpha): An Acid Phosphatase with Purine Nucleotide Specificity
J.Mol.Biol., 326:1559-1575, 2003

PubMed Abstract: The survival protein E (SurE) family was discovered by its correlation to stationary phase survival of Escherichia coli and various repair proteins involved in sustaining this and other stress-response phenotypes. In order to better understand this ancient and well-conserved protein family, we have determined the 2.0A resolution crystal structure of SurEalpha from the hyperthermophilic crenarchaeon Pyrobaculum aerophilum (Pae). This first structure of an archaeal SurE reveals significant similarities to and differences from the only other known SurE structure, that from the eubacterium Thermatoga maritima (Tma). Both SurE monomers adopt similar folds; however, unlike the Tma SurE dimer, crystalline Pae SurEalpha is predominantly non-domain swapped. Comparative structural analyses of Tma and Pae SurE suggest conformationally variant regions, such as a hinge loop that may be involved in domain swapping. The putative SurE active site is highly conserved, and implies a model for SurE bound to a potential substrate, guanosine-5'-monophosphate (GMP). Pae SurEalpha has optimal acid phosphatase activity at temperatures above 90 degrees C, and is less specific than Tma SurE in terms of metal ion requirements. Substrate specificity also differs between Pae and Tma SurE, with a more specific recognition of purine nucleotides by the archaeal enzyme. Analyses of the sequences, phylogenetic distribution, and genomic organization of the SurE family reveal examples of genomes encoding multiple surE genes, and suggest that SurE homologs constitute a broad family of enzymes with phosphatase-like activities.

PubMed: 12595266

Experimental method

X-RAY DIFFRACTION (2 Å)