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1ilv

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(New page: 200px<br /><applet load="1ilv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ilv, resolution 2.00&Aring;" /> '''Crystal Structure An...)
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Revision as of 15:22, 20 November 2007


1ilv, resolution 2.00Å

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Crystal Structure Analysis of the TM107

Overview

BACKGROUND: The 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. RESULTS: The 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., CONCLUSIONS: The 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.

About this Structure

1ILV is a Single protein structure of sequence from Thermotoga maritima. Full crystallographic information is available from OCA.

Reference

Structure of Thermotoga maritima stationary phase survival protein SurE: a novel acid phosphatase., Zhang RG, Skarina T, Katz JE, Beasley S, Khachatryan A, Vyas S, Arrowsmith CH, Clarke S, Edwards A, Joachimiak A, Savchenko A, Structure. 2001 Nov;9(11):1095-106. PMID:11709173

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