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New page: left|200px<br /><applet load="1ilv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ilv, resolution 2.00Å" /> '''Crystal Structure An...
 
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[[Image:1ilv.gif|left|200px]]<br /><applet load="1ilv" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1ilv.gif|left|200px]]<br /><applet load="1ilv" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1ilv, resolution 2.00&Aring;" />
caption="1ilv, resolution 2.00&Aring;" />
'''Crystal Structure Analysis of the TM107'''<br />
'''Crystal Structure Analysis of the TM107'''<br />


==Overview==
==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.
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==
==About this Structure==
1ILV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ILV OCA].  
1ILV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ILV OCA].  


==Reference==
==Reference==
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[[Category: Evdokimova, E.]]
[[Category: Evdokimova, E.]]
[[Category: Joachimiak, A.]]
[[Category: Joachimiak, A.]]
[[Category: MCSG, Midwest.Center.for.Structural.Genomics.]]
[[Category: MCSG, Midwest Center for Structural Genomics.]]
[[Category: Savchenko, A.]]
[[Category: Savchenko, A.]]
[[Category: Zhang, R.]]
[[Category: Zhang, R.]]
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[[Category: structural genomics ]]
[[Category: structural genomics ]]


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