1ilv
From Proteopedia
(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...) |
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| - | [[Image:1ilv.gif|left|200px]]<br /><applet load="1ilv" size=" | + | [[Image:1ilv.gif|left|200px]]<br /><applet load="1ilv" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ilv, resolution 2.00Å" /> | caption="1ilv, resolution 2.00Å" /> | ||
'''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 | + | 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:// | + | 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 | + | [[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 ]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:13:16 2008'' |
Revision as of 11:13, 21 February 2008
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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
Page seeded by OCA on Thu Feb 21 13:13:16 2008
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
