This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1ilv
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /><applet load="1ilv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ilv, resolution 2.00Å" /> '''Crystal Structure An...)
Next diff →
Revision as of 15:22, 20 November 2007
|
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
Page seeded by OCA on Tue Nov 20 17:29:32 2007
Categories: Single protein | Thermotoga maritima | Beasley, S. | Edwards, A. | Evdokimova, E. | Joachimiak, A. | MCSG, Midwest.Center.for.Structural.Genomics. | Savchenko, A. | Zhang, R. | Mcsg | Midwest center for structural genomics | New fold | Protein structure initiative | Psi | Structural genomics
