2btm

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(New page: 200px<br /><applet load="2btm" size="450" color="white" frame="true" align="right" spinBox="true" caption="2btm, resolution 2.4&Aring;" /> '''DOES THE HIS12-LYS13 ...)
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[[Image:2btm.gif|left|200px]]<br /><applet load="2btm" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2btm, resolution 2.4&Aring;" />
 
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'''DOES THE HIS12-LYS13 PAIR PLAY A ROLE IN THE ADAPTATION OF THERMOPHILIC TIMS TO HIGH TEMPERATURES?'''<br />
 
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==Overview==
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==DOES THE HIS12-LYS13 PAIR PLAY A ROLE IN THE ADAPTATION OF THERMOPHILIC TIMS TO HIGH TEMPERATURES?==
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The thermophilic triose-phosphate isomerases (TIMs) of Bacillus, stearothermophilus (bTIM) and Thermotoga maritima (tTIM) have been found, to possess a His12-Lys13 pair instead of the Asn12-Gly13 pair normally, present in mesophilic TIMs. His12 in bTIM was proposed to prevent, deamidation at high temperature, while the precise role of Lys13 is, unknown. To investigate the role of the His12 and Lys13 pair in the, enzyme's thermoadaptation, we reintroduced the "mesophilic residues" Asn, and Gly into both thermophilic TIMs. Neither double mutant displayed, diminished structural stability, but the bTIM double mutant showed, drastically reduced catalytic activity. No similar behavior was observed, with the tTIM double mutant, suggesting that the presence of the His12 and, Lys13 cannot be systematically correlated to thermoadaptation in TIMs. We, determined the crystal structure of the bTIM double mutant complexed with, 2-phosphoglycolate to 2.4-A resolution. A molecular dynamics simulation, showed that upon substitution of Lys13 to Gly an increase of the, flexibility of loop 1 is observed, causing an incorrect orientation of the, catalytic Lys10. This suggests that Lys13 in bTIM plays a crucial role in, the functional adaptation of this enzyme to high temperature. Analysis of, bTIM single mutants supports this assumption.
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<StructureSection load='2btm' size='340' side='right'caption='[[2btm]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2btm]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BTM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BTM FirstGlance]. <br>
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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]] 2.4&#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=PGA:2-PHOSPHOGLYCOLIC+ACID'>PGA</scene></td></tr>
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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=2btm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2btm OCA], [https://pdbe.org/2btm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2btm RCSB], [https://www.ebi.ac.uk/pdbsum/2btm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2btm ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/TPIS_GEOSE TPIS_GEOSE]
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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/bt/2btm_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=2btm ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The thermophilic triose-phosphate isomerases (TIMs) of Bacillus stearothermophilus (bTIM) and Thermotoga maritima (tTIM) have been found to possess a His12-Lys13 pair instead of the Asn12-Gly13 pair normally present in mesophilic TIMs. His12 in bTIM was proposed to prevent deamidation at high temperature, while the precise role of Lys13 is unknown. To investigate the role of the His12 and Lys13 pair in the enzyme's thermoadaptation, we reintroduced the "mesophilic residues" Asn and Gly into both thermophilic TIMs. Neither double mutant displayed diminished structural stability, but the bTIM double mutant showed drastically reduced catalytic activity. No similar behavior was observed with the tTIM double mutant, suggesting that the presence of the His12 and Lys13 cannot be systematically correlated to thermoadaptation in TIMs. We determined the crystal structure of the bTIM double mutant complexed with 2-phosphoglycolate to 2.4-A resolution. A molecular dynamics simulation showed that upon substitution of Lys13 to Gly an increase of the flexibility of loop 1 is observed, causing an incorrect orientation of the catalytic Lys10. This suggests that Lys13 in bTIM plays a crucial role in the functional adaptation of this enzyme to high temperature. Analysis of bTIM single mutants supports this assumption.
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==About this Structure==
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Lys13 plays a crucial role in the functional adaptation of the thermophilic triose-phosphate isomerase from Bacillus stearothermophilus to high temperatures.,Alvarez M, Wouters J, Maes D, Mainfroid V, Rentier-Delrue F, Wyns L, Depiereux E, Martial JA J Biol Chem. 1999 Jul 2;274(27):19181-7. PMID:10383424<ref>PMID:10383424</ref>
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2BTM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus] with PGA as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Triose-phosphate_isomerase Triose-phosphate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.1 5.3.1.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BTM OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Lys13 plays a crucial role in the functional adaptation of the thermophilic triose-phosphate isomerase from Bacillus stearothermophilus to high temperatures., Alvarez M, Wouters J, Maes D, Mainfroid V, Rentier-Delrue F, Wyns L, Depiereux E, Martial JA, J Biol Chem. 1999 Jul 2;274(27):19181-7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10383424 10383424]
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</div>
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[[Category: Geobacillus stearothermophilus]]
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<div class="pdbe-citations 2btm" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Triose-phosphate isomerase]]
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[[Category: Delboni, L.F.]]
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[[Category: Hol, W.G.J.]]
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[[Category: Mande, S.C.]]
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[[Category: PGA]]
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[[Category: glycolysis]]
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[[Category: thermophilic triose-phosphate]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 08:54:49 2007''
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==See Also==
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*[[Triose phosphate isomerase 3D structures|Triose phosphate isomerase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Geobacillus stearothermophilus]]
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[[Category: Large Structures]]
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[[Category: Delboni LF]]
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[[Category: Hol WGJ]]
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[[Category: Mande SC]]

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DOES THE HIS12-LYS13 PAIR PLAY A ROLE IN THE ADAPTATION OF THERMOPHILIC TIMS TO HIGH TEMPERATURES?

PDB ID 2btm

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