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New page: left|200px<br /><applet load="1tti" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tti, resolution 2.4Å" /> '''THREE NEW CRYSTAL STR...
 
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[[Image:1tti.gif|left|200px]]<br /><applet load="1tti" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1tti, resolution 2.4&Aring;" />
'''THREE NEW CRYSTAL STRUCTURES OF POINT MUTATION VARIANTS OF MONOTIM: CONFORMATIONAL FLEXIBILITY OF LOOP-1,LOOP-4 AND LOOP-8'''<br />


==Overview==
==THREE NEW CRYSTAL STRUCTURES OF POINT MUTATION VARIANTS OF MONOTIM: CONFORMATIONAL FLEXIBILITY OF LOOP-1,LOOP-4 AND LOOP-8==
BACKGROUND: Wild-type triosephosphate isomerase (TIM) is a very stable, dimeric enzyme. This dimer can be converted into a stable monomeric, protein (monoTIM) by replacing the 15-residue interface loop (loop-3) by a, shorter, 8-residue, loop. The crystal structure of monoTIM shows that two, active-site loops (loop-1 and loop-4), which are at the dimer interface in, wild-type TIM, have acquired rather different structural properties., Nevertheless, monoTIM has residual catalytic activity. RESULTS: Three new, structures of variants of monoTIM are presented, a double-point mutant, crystallized in the presence and absence of bound inhibitor, and a, single-point mutant in the presence of a different inhibitor. These new, structures show large structural variability for the active-site loops, loop-1, loop-4 and loop-8. In the structures with inhibitor bound, the, catalytic lysine (Lys13 in loop-1) and the catalytic histidine (His95 in, loop-4) adopt conformations similar to those observed in wild-type TIM, but very different from the monoTIM structure. CONCLUSIONS: The residual, catalytic activity of monoTIM can now be rationalized. In the presence of, substrate analogues the active-site loops, loop-1, loop-4 and loop-8, as, well as the catalytic residues, adopt conformations similar to those seen, in the wild-type protein. These loops lack conformational flexibility in, wild-type TIM. The data suggest that the rigidity of these loops in, wild-type TIM, resulting from subunit-subunit contacts at the dimer, interface, is important for optimal catalysis.
<StructureSection load='1tti' size='340' side='right'caption='[[1tti]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1tti]] 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=1TTI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TTI 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=PGA:2-PHOSPHOGLYCOLIC+ACID'>PGA</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=1tti FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tti OCA], [https://pdbe.org/1tti PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tti RCSB], [https://www.ebi.ac.uk/pdbsum/1tti PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tti 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/tt/1tti_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=1tti ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1TTI 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 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=1TTI OCA].
*[[Triose phosphate isomerase 3D structures|Triose phosphate isomerase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Three new crystal structures of point mutation variants of monoTIM: conformational flexibility of loop-1, loop-4 and loop-8., Borchert TV, Kishan KV, Zeelen JP, Schliebs W, Thanki N, Abagyan R, Jaenicke R, Wierenga RK, Structure. 1995 Jul 15;3(7):669-79. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8591044 8591044]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Triose-phosphate isomerase]]
[[Category: Trypanosoma brucei brucei]]
[[Category: Trypanosoma brucei brucei]]
[[Category: Kishan, K.V.Radha.]]
[[Category: Radha Kishan KV]]
[[Category: Wierenga, R.K.]]
[[Category: Wierenga RK]]
[[Category: PGA]]
[[Category: isomerase(intramolecular oxidoreductase)]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:34:50 2007''

Latest revision as of 08:41, 14 February 2024

THREE NEW CRYSTAL STRUCTURES OF POINT MUTATION VARIANTS OF MONOTIM: CONFORMATIONAL FLEXIBILITY OF LOOP-1,LOOP-4 AND LOOP-8

1tti, resolution 2.40Å

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