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New page: left|200px<br /><applet load="1tri" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tri, resolution 2.4Å" /> '''THE CRYSTAL STRUCTURE...
 
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[[Image:1tri.gif|left|200px]]<br /><applet load="1tri" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1tri, resolution 2.4&Aring;" />
'''THE CRYSTAL STRUCTURE OF AN ENGINEERED MONOMERIC TRIOSEPHOSPHATE ISOMERASE, MONOTIM: THE CORRECT MODELLING OF AN EIGHT-RESIDUE LOOP'''<br />


==Overview==
==THE CRYSTAL STRUCTURE OF AN ENGINEERED MONOMERIC TRIOSEPHOSPHATE ISOMERASE, MONOTIM: THE CORRECT MODELLING OF AN EIGHT-RESIDUE LOOP==
BACKGROUND: The triosephosphate isomerase (TIM) fold is found in several, different classes of enzymes, most of which are oligomers; TIM itself, always functions as a very tight dimer. It has recently been shown that a, monomeric form of TIM ('monoTIM') can be constructed by replacing a, 15-residue interface loop, loop-3, with an eight-residue fragment;, modelling suggests that this should result in a short strain-free turn, resulting in the subsequent helix, helix-A3, having an additional turn at, its amino terminus. RESULTS: The crystal structure of monoTIM shows that, it retains the characteristic TIM-barrel (betaalpha)8-fold and that the, new loop has a structure very close to that predicted. Two other interface, loops, loop-1 and loop-4, which contain the active site residues Lys13 and, His95, respectively, show significant changes in structure in monoTIM, compared with dimeric wild-type TIM. CONCLUSION: The observed structural, differences between monoTIM and wild-type TIM indicate that the dimeric, appearance of TIM determines the location and conformation of two of the, four catalytic residues.
<StructureSection load='1tri' size='340' side='right'caption='[[1tri]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1tri]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Trypanosoma_brucei_brucei Trypanosoma brucei brucei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TRI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TRI 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]] 2.4&#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=1tri FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tri OCA], [https://pdbe.org/1tri PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tri RCSB], [https://www.ebi.ac.uk/pdbsum/1tri PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tri ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TPIS_TRYBB TPIS_TRYBB]
== 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/tr/1tri_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=1tri ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1TRI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Trypanosoma_brucei_brucei Trypanosoma brucei brucei] 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=1TRI OCA].
*[[Triose phosphate isomerase 3D structures|Triose phosphate isomerase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
The crystal structure of an engineered monomeric triosephosphate isomerase, monoTIM: the correct modelling of an eight-residue loop., Borchert TV, Abagyan R, Kishan KV, Zeelen JP, Wierenga RK, Structure. 1993 Nov 15;1(3):205-13. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16100954 16100954]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Triose-phosphate isomerase]]
[[Category: Trypanosoma brucei brucei]]
[[Category: Trypanosoma brucei brucei]]
[[Category: Wierenga, R.K.]]
[[Category: Wierenga RK]]
[[Category: SO4]]
[[Category: isomerase(intramolecular oxidoreductase)]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:32:15 2007''

Latest revision as of 08:41, 14 February 2024

THE CRYSTAL STRUCTURE OF AN ENGINEERED MONOMERIC TRIOSEPHOSPHATE ISOMERASE, MONOTIM: THE CORRECT MODELLING OF AN EIGHT-RESIDUE LOOP

1tri, resolution 2.40Å

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