1w0m: Difference between revisions

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-[[Image:1w0m.gif|left|200px]]
- {{Structure
+==Triosephosphate isomerase from Thermoproteus tenax==
-|PDB= 1w0m |SIZE=350|CAPTION= <scene name='initialview01'>1w0m</scene>, resolution 2.5&Aring;
+<StructureSection load='1w0m' size='340' side='right'caption='[[1w0m]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
-|SITE= <scene name='pdbsite=AC1:Po4+Binding+Site+For+Chain+H'>AC1</scene>
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=PO4:PHOSPHATE ION'>PO4</scene>
+<table><tr><td colspan='2'>[[1w0m]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermoproteus_tenax Thermoproteus tenax]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W0M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1W0M FirstGlance]. <br>
-|ACTIVITY= [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]
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
-|GENE=
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
-}}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1w0m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w0m OCA], [https://pdbe.org/1w0m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1w0m RCSB], [https://www.ebi.ac.uk/pdbsum/1w0m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1w0m ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/TPIS_THETK TPIS_THETK]
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/w0/1w0m_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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=1w0m ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Triosephophate isomerase (TIM) is a dimeric enzyme in eucarya, bacteria and mesophilic archaea. In hyperthermophilic archaea, however, TIM exists as a tetramer composed of monomers that are about 10% shorter than other eucaryal and bacterial TIM monomers. We report here the crystal structure of TIM from Thermoproteus tenax, a hyperthermophilic archaeon that has an optimum growth temperature of 86 degrees C. The structure was determined from both a hexagonal and an orthorhombic crystal form to resolutions of 2.5A and 2.3A, and refined to R-factors of 19.7% and 21.5%, respectively. In both crystal forms, T.tenax TIM exists as a tetramer of the familiar (betaalpha)(8)-barrel. In solution, however, and unlike other hyperthermophilic TIMs, the T.tenax enzyme exhibits an equilibrium between inactive dimers and active tetramers, which is shifted to the tetramer state through a specific interaction with glycerol-1-phosphate dehydrogenase of T.tenax. This observation is interpreted in physiological terms as a need to reduce the build-up of thermolabile metabolic intermediates that would be susceptible to destruction by heat. A detailed structural comparison with TIMs from organisms with growth optima ranging from 15 degrees C to 100 degrees C emphasizes the importance in hyperthermophilic proteins of the specific location of ionic interactions for thermal stability rather than their numbers, and shows a clear correlation between the reduction of heat-labile, surface-exposed Asn and Gln residues with thermoadaptation. The comparison confirms the increase in charged surface-exposed residues at the expense of polar residues.
-'''TRIOSEPHOSPHATE ISOMERASE FROM THERMOPROTEUS TENAX'''
+Structure and function of a regulated archaeal triosephosphate isomerase adapted to high temperature.,Walden H, Taylor GL, Lorentzen E, Pohl E, Lilie H, Schramm A, Knura T, Stubbe K, Tjaden B, Hensel R J Mol Biol. 2004 Sep 17;342(3):861-75. PMID:15342242<ref>PMID:15342242</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1w0m" style="background-color:#fffaf0;"></div>
-==Overview==
+==See Also==
-Triosephophate isomerase (TIM) is a dimeric enzyme in eucarya, bacteria and mesophilic archaea. In hyperthermophilic archaea, however, TIM exists as a tetramer composed of monomers that are about 10% shorter than other eucaryal and bacterial TIM monomers. We report here the crystal structure of TIM from Thermoproteus tenax, a hyperthermophilic archaeon that has an optimum growth temperature of 86 degrees C. The structure was determined from both a hexagonal and an orthorhombic crystal form to resolutions of 2.5A and 2.3A, and refined to R-factors of 19.7% and 21.5%, respectively. In both crystal forms, T.tenax TIM exists as a tetramer of the familiar (betaalpha)(8)-barrel. In solution, however, and unlike other hyperthermophilic TIMs, the T.tenax enzyme exhibits an equilibrium between inactive dimers and active tetramers, which is shifted to the tetramer state through a specific interaction with glycerol-1-phosphate dehydrogenase of T.tenax. This observation is interpreted in physiological terms as a need to reduce the build-up of thermolabile metabolic intermediates that would be susceptible to destruction by heat. A detailed structural comparison with TIMs from organisms with growth optima ranging from 15 degrees C to 100 degrees C emphasizes the importance in hyperthermophilic proteins of the specific location of ionic interactions for thermal stability rather than their numbers, and shows a clear correlation between the reduction of heat-labile, surface-exposed Asn and Gln residues with thermoadaptation. The comparison confirms the increase in charged surface-exposed residues at the expense of polar residues.
+*[[Triose phosphate isomerase 3D structures|Triose phosphate isomerase 3D structures]]
+== References ==
-==About this Structure==
+<references/>
-W0M is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermoproteus_tenax Thermoproteus tenax]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W0M OCA].
+__TOC__
+</StructureSection>
-==Reference==
+[[Category: Large Structures]]
-Structure and function of a regulated archaeal triosephosphate isomerase adapted to high temperature., Walden H, Taylor GL, Lorentzen E, Pohl E, Lilie H, Schramm A, Knura T, Stubbe K, Tjaden B, Hensel R, J Mol Biol. 2004 Sep 17;342(3):861-75. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15342242 15342242]
-[[Category: Single protein]]
 [[Category: Thermoproteus tenax]]
-[[Category: Triose-phosphate isomerase]]
+[[Category: Hensel R]]
-[[Category: Hensel, R.]]
+[[Category: Knura T]]
-[[Category: Knura, T.]]
+[[Category: Lilie H]]
-[[Category: Lilie, H.]]
+[[Category: Lorentzen E]]
-[[Category: Lorentzen, E.]]
+[[Category: Pohl E]]
-[[Category: Pohl, E.]]
+[[Category: Schramm A]]
-[[Category: Schramm, A.]]
+[[Category: Stubbe K]]
-[[Category: Stubbe, K.]]
+[[Category: Taylor G]]
-[[Category: Taylor, G.]]
+[[Category: Tjaden B]]
-[[Category: Tjaden, B.]]
+[[Category: Walden H]]
-[[Category: Walden, H.]]
-[[Category: PO4]]
-[[Category: gluconeogenesis]]
-[[Category: glycolysis]]
-[[Category: triosephosphate isomerase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:50:32 2008''