1tmh: Difference between revisions

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OCA

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-[[Image:1tmh.gif|left|200px]]<br /><applet load="1tmh" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1tmh, resolution 2.8&Aring;" />
-'''MODULAR MUTAGENESIS OF A TIM-BARREL ENZYME: THE CRYSTAL STRUCTURE OF A CHIMERIC E. COLI TIM HAVING THE EIGHTH (BETA-ALPHA)-UNIT REPLACED BY THE EQUIVALENT UNIT OF CHICKEN TIM'''<br />
-==Overview==
+==MODULAR MUTAGENESIS OF A TIM-BARREL ENZYME: THE CRYSTAL STRUCTURE OF A CHIMERIC E. COLI TIM HAVING THE EIGHTH (BETA-ALPHA)-UNIT REPLACED BY THE EQUIVALENT UNIT OF CHICKEN TIM==
-The crystal structure of a hybrid Escherichia coli triosephosphate, isomerase (TIM) has been determined at 2.8 A resolution. The hybrid TIM, (ETIM8CHI) was constructed by replacing the eighth beta alpha-unit of E., coli TIM with the equivalent unit of chicken TIM. This replacement, involves 10 sequence changes. One of the changes concerns the mutation of, a buried alanine (Ala232 in strand 8) into a phenylalanine. The ETIM8CHI, structure shows that the A232F sequence change can be incorporated by a, side-chain rotation of Phe224 (in helix 7). No cavities or strained, dihedrals are observed in ETIM8CHI in the region near position 232, which, is in agreement with the observation that ETIM8CHI and E.coli TIM have, similar stabilities. The largest CA (C-alpha atom) movements, approximately 3 A, are seen for the C-terminal end of helix 8 (associated, with the outward rotation of Phe224) and for the residues in the loop, after helix 1 (associated with sequence changes in helix 8). From the, structure it is not clear why the kcat of ETIM8CHI is 10 times lower than, in wild type E.coli TIM.
+<StructureSection load='1tmh' size='340' side='right'caption='[[1tmh]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1tmh]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TMH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TMH FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1tmh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tmh OCA], [https://pdbe.org/1tmh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tmh RCSB], [https://www.ebi.ac.uk/pdbsum/1tmh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tmh ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/TPIS_ECOLI TPIS_ECOLI] [https://www.uniprot.org/uniprot/TPIS_CHICK TPIS_CHICK]
+== 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/tm/1tmh_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=1tmh ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-TMH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with SO4 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=1TMH OCA].
+*[[Triose phosphate isomerase 3D structures|Triose phosphate isomerase 3D structures]]
+__TOC__
-==Reference==
+</StructureSection>
-Modular mutagenesis of a TIM-barrel enzyme: the crystal structure of a chimeric E. coli TIM having the eighth beta alpha-unit replaced by the equivalent unit of chicken TIM., Kishan R, Zeelen JP, Noble ME, Borchert TV, Mainfroid V, Goraj K, Martial JA, Wierenga RK, Protein Eng. 1994 Aug;7(8):945-51. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7809033 7809033]
 [[Category: Escherichia coli]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Triose-phosphate isomerase]]
+[[Category: Radha Kishan KV]]
-[[Category: Kishan, K.V.Radha.]]
+[[Category: Wierenga RK]]
-[[Category: Wierenga, R.K.]]
+[[Category: Zeelen JPh]]
-[[Category: Zeelen, J.Ph.]]
-[[Category: SO4]]
-[[Category: isomerase(intramolecular oxidoreductase)]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:24:39 2007''