ArticleStructure (London, England : 1993)2001
Structure of Thermotoga maritima stationary phase survival protein SurE: a novel acid phosphatase.
Article in Structure (London, England : 1993), 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.
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Who cites it
72 citing papers in PubMed, 109 citations in OpenAlex.
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- Structural and functional characterization of the TYW3/Taw3 class of SAM-dependent methyltransferases.RNA (New York, N.Y.) · 2017Article
- Structural and functional insights into the stationary-phase survival protein SurE, an important virulence factor of Brucella abortus.Acta crystallographica. Section F, Structural biology communications · 2016Article
- Experimental validation of in silico model-predicted isocitrate dehydrogenase and phosphomannose isomerase from Dehalococcoides mccartyi.Microbial biotechnology · 2016Article
- Functional Diversity of Haloacid Dehalogenase Superfamily Phosphatases from Saccharomyces cerevisiae: BIOCHEMICAL, STRUCTURAL, AND EVOLUTIONARY INSIGHTS.The Journal of biological chemistry · 2015Article
- Transcription level analysis of intracellular Burkholderia pseudomallei illustrates the role of BPSL1502 during bacterial interaction with human lung epithelial cells.Journal of microbiology (Seoul, Korea) · 2015Article
- Double trouble-Buffer selection and His-tag presence may be responsible for nonreproducibility of biomedical experiments.Protein science : a publication of the Protein Society · 2014Article
- Assembly principles of a unique cage formed by hexameric and decameric E. coli proteins.eLife · 2014Article
- The crystal structure of pyrimidine/thiamin biosynthesis precursor-like domain-containing protein CAE31940 from proteobacterium Bordetella bronchiseptica RB50, and evolutionary insight into the NMT1/THI5 family.Journal of structural and functional genomics · 2014Article
- Structural characterization of a hypothetical protein: a potential agent involved in trimethylamine metabolism in Catenulispora acidiphila.Journal of structural and functional genomics · 2014Article
- The Legionella pneumophila kai operon is implicated in stress response and confers fitness in competitive environments.Environmental microbiology · 2014Article
- The MoxR ATPase RavA and its cofactor ViaA interact with the NADH:ubiquinone oxidoreductase I in Escherichia coli.PloS one · 2014Article
- Biochemical studies of the multicopper oxidase (small laccase) from Streptomyces coelicolor using bioactive phytochemicals and site-directed mutagenesis.Microbial biotechnology · 2013Article
- Structural and functional insight into the universal stress protein family.Evolutionary applications · 2013Article
12 more citing papers are in PubMed but not listed here.
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Authors and funding
11 authors at 4 institutions in 2 countries.
Funding
Abstract
backgroundThe rpoS, nlpD, pcm, and surE genes are among many whose expression is induced during the stationary phase of bacterial growth. rpoS codes for the stationary-phase RNA polymerase sigma subunit, and nlpD codes for a lipoprotein. The pcm gene product repairs damaged proteins by converting the atypical isoaspartyl residues back to L-aspartyls. The physiological and biochemical functions of surE are unknown, but its importance in stress is supported by the duplication of the surE gene in E. coli subjected to high-temperature growth. The pcm and surE genes are highly conserved in bacteria, archaea, and plants.
resultsThe structure of SurE from Thermotoga maritima was determined at 2.0 A. The SurE monomer is composed of two domains; a conserved N-terminal domain, a Rossman fold, and a C-terminal oligomerization domain, a new fold. Monomers form a dimer that assembles into a tetramer. Biochemical analysis suggests that SurE is an acid phosphatase, with an optimum pH of 5.5-6.2. The active site was identified in the N-terminal domain through analysis of conserved residues. Structure-based site-directed point mutations abolished phosphatase activity. T. maritima SurE intra- and intersubunit salt bridges were identified that may explain the SurE thermostability.
conclusionsThe structure of SurE provided information about the protein's fold, oligomeric state, and active site. The protein possessed magnesium-dependent acid phosphatase activity, but the physiologically relevant substrate(s) remains to be identified. The importance of three of the assigned active site residues in catalysis was confirmed by site-directed mutagenesis.
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