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1ilv

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(New page: 200px<br /><applet load="1ilv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ilv, resolution 2.00&Aring;" /> '''Crystal Structure An...)
Current revision (06:02, 3 April 2024) (edit) (undo)
 
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[[Image:1ilv.gif|left|200px]]<br /><applet load="1ilv" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ilv, resolution 2.00&Aring;" />
 
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'''Crystal Structure Analysis of the TM107'''<br />
 
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==Overview==
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==Crystal Structure Analysis of the TM107==
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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.
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<StructureSection load='1ilv' size='340' side='right'caption='[[1ilv]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1ilv]] is a 2 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ILV FirstGlance]. <br>
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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].
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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==Reference==
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ilv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ilv OCA], [https://pdbe.org/1ilv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ilv RCSB], [https://www.ebi.ac.uk/pdbsum/1ilv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ilv ProSAT], [https://www.topsan.org/Proteins/MCSG/1ilv TOPSAN]</span></td></tr>
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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]
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</table>
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[[Category: Single protein]]
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== Function ==
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[https://www.uniprot.org/uniprot/SURE_THEMA SURE_THEMA] Nucleotidase that preferentially dephosphorylates 5'-GMP and 5'-AMP.[HAMAP-Rule:MF_00060]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/il/1ilv_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ilv ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Thermotoga maritima]]
[[Category: Thermotoga maritima]]
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[[Category: Beasley, S.]]
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[[Category: Beasley S]]
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[[Category: Edwards, A.]]
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[[Category: Edwards A]]
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[[Category: Evdokimova, E.]]
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[[Category: Evdokimova E]]
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[[Category: Joachimiak, A.]]
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[[Category: Joachimiak A]]
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[[Category: MCSG, Midwest.Center.for.Structural.Genomics.]]
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[[Category: Savchenko A]]
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[[Category: Savchenko, A.]]
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[[Category: Zhang R]]
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[[Category: Zhang, R.]]
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[[Category: mcsg]]
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[[Category: midwest center for structural genomics]]
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[[Category: new fold]]
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[[Category: protein structure initiative]]
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[[Category: psi]]
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[[Category: structural genomics ]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:29:32 2007''
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Current revision

Crystal Structure Analysis of the TM107

PDB ID 1ilv

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