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| - | [[Image:1ilv.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1ilv| PDB=1ilv | SCENE= }} | | {{STRUCTURE_1ilv| PDB=1ilv | SCENE= }} |
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| - | '''Crystal Structure Analysis of the TM107'''
| + | ===Crystal Structure Analysis of the TM107=== |
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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_11709173}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11709173 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_11709173}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Psi]] | | [[Category: Psi]] |
| | [[Category: Structural genomic]] | | [[Category: Structural genomic]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:08:15 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 13:29:20 2008'' |
Revision as of 10:29, 1 July 2008
Template:STRUCTURE 1ilv
Crystal Structure Analysis of the TM107
Template:ABSTRACT PUBMED 11709173
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 Jul 1 13:29:20 2008
