1ilv: Difference between revisions

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[[Image:1ilv.gif|left|200px]]<br /><applet load="1ilv" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1ilv.gif|left|200px]]
caption="1ilv, resolution 2.00&Aring;" />
 
'''Crystal Structure Analysis of the TM107'''<br />
{{Structure
|PDB= 1ilv |SIZE=350|CAPTION= <scene name='initialview01'>1ilv</scene>, resolution 2.00&Aring;
|SITE=
|LIGAND=
|ACTIVITY=
|GENE=
}}
 
'''Crystal Structure Analysis of the TM107'''
 


==Overview==
==Overview==
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==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://oca.weizmann.ac.il/oca-bin/ocashort?id=1ILV OCA].  
1ILV is a [[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==
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11709173 11709173]
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:[http://www.ncbi.nlm.nih.gov/pubmed/11709173 11709173]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Thermotoga maritima]]
[[Category: Thermotoga maritima]]
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[[Category: Zhang, R.]]
[[Category: Zhang, R.]]
[[Category: mcsg]]
[[Category: mcsg]]
[[Category: midwest center for structural genomics]]
[[Category: midwest center for structural genomic]]
[[Category: new fold]]
[[Category: new fold]]
[[Category: protein structure initiative]]
[[Category: protein structure initiative]]
[[Category: psi]]
[[Category: psi]]
[[Category: structural genomics ]]
[[Category: structural genomic]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:51:58 2008''

Revision as of 09:51, 20 March 2008

File:1ilv.gif


Drag the structure with the mouse to rotate
1ilv, resolution 2.00Å
Coordinates: save as pdb, mmCIF, xml



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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