1su5
From Proteopedia
(Difference between revisions)
(New page: 200px<br /><applet load="1su5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1su5, resolution 2.70Å" /> '''Understanding protei...) |
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| - | [[Image:1su5.jpg|left|200px]]<br /><applet load="1su5" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1su5, resolution 2.70Å" /> | ||
| - | '''Understanding protein lids: Structural analysis of active hinge mutants in triosephosphate isomerase'''<br /> | ||
| - | == | + | ==Understanding protein lids: Structural analysis of active hinge mutants in triosephosphate isomerase== |
| - | The conformational switch from open to closed of the flexible loop 6 of | + | <StructureSection load='1su5' size='340' side='right'caption='[[1su5]], [[Resolution|resolution]] 2.70Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1su5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SU5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SU5 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]] 2.7Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PGA:2-PHOSPHOGLYCOLIC+ACID'>PGA</scene>, <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=1su5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1su5 OCA], [https://pdbe.org/1su5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1su5 RCSB], [https://www.ebi.ac.uk/pdbsum/1su5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1su5 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [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/su/1su5_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=1su5 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The conformational switch from open to closed of the flexible loop 6 of triosephosphate isomerase (TIM) is essential for the catalytic properties of TIM. Using a directed evolution approach, active variants of chicken TIM with a mutated C-terminal hinge tripeptide of loop 6 have been generated (Sun,J. and Sampson,N.S., Biochemistry, 1999, 38, 11474-11481). In chicken TIM, the wild-type C-terminal hinge tripeptide is KTA. Detailed enzymological characterization of six variants showed that some of these (LWA, NPN, YSL, KTK) have decreased catalytic efficiency, whereas others (KVA, NSS) are essentially identical with wild-type. The structural characterization of these six variants is reported. No significant structural differences compared with the wild-type are found for KVA, NSS and LWA, but substantial structural adaptations are seen for NPN, YSL and KTK. These structural differences can be understood from the buried position of the alanine side chain in the C-hinge position 3 in the open conformation of wild-type loop 6. Replacement of this alanine with a bulky side chain causes the closed conformation to be favored, which correlates with the decreased catalytic efficiency of these variants. The structural context of loop 6 and loop 7 and their sequence conservation in 133 wild-type sequences is also discussed. | ||
| - | + | Understanding protein lids: structural analysis of active hinge mutants in triosephosphate isomerase.,Kursula I, Salin M, Sun J, Norledge BV, Haapalainen AM, Sampson NS, Wierenga RK Protein Eng Des Sel. 2004 Apr;17(4):375-82. Epub 2004 May 27. PMID:15166315<ref>PMID:15166315</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1su5" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[Triose phosphate isomerase 3D structures|Triose phosphate isomerase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Gallus gallus]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Haapalainen AM]] | ||
| + | [[Category: Kursula I]] | ||
| + | [[Category: Norledge BV]] | ||
| + | [[Category: Salin M]] | ||
| + | [[Category: Sampson NS]] | ||
| + | [[Category: Sun J]] | ||
| + | [[Category: Wierenga RK]] | ||
Current revision
Understanding protein lids: Structural analysis of active hinge mutants in triosephosphate isomerase
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