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| | ==Triosephosphate isomerase from Gallus gallus, loop 6 mutant K174N, T175S, A176S== | | ==Triosephosphate isomerase from Gallus gallus, loop 6 mutant K174N, T175S, A176S== |
| - | <StructureSection load='1sw7' size='340' side='right' caption='[[1sw7]], [[Resolution|resolution]] 2.22Å' scene=''> | + | <StructureSection load='1sw7' size='340' side='right'caption='[[1sw7]], [[Resolution|resolution]] 2.22Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1sw7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Chick Chick]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SW7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1SW7 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1sw7]] 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=1SW7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SW7 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PGA:2-PHOSPHOGLYCOLIC+ACID'>PGA</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.22Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1spq|1spq]], [[1sq7|1sq7]], [[1ssd|1ssd]], [[1ssg|1ssg]], [[1su5|1su5]], [[1sw0|1sw0]], [[1sw3|1sw3]]</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TPI1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9031 CHICK])</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=1sw7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sw7 OCA], [https://pdbe.org/1sw7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sw7 RCSB], [https://www.ebi.ac.uk/pdbsum/1sw7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sw7 ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
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| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1sw7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sw7 OCA], [http://pdbe.org/1sw7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1sw7 RCSB], [http://www.ebi.ac.uk/pdbsum/1sw7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1sw7 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/TPIS_CHICK TPIS_CHICK] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[Triose Phosphate Isomerase|Triose Phosphate Isomerase]] | + | *[[Triose phosphate isomerase 3D structures|Triose phosphate isomerase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Chick]] | + | [[Category: Gallus gallus]] |
| - | [[Category: Triose-phosphate isomerase]] | + | [[Category: Large Structures]] |
| - | [[Category: Haapalainen, A M]] | + | [[Category: Haapalainen AM]] |
| - | [[Category: Kursula, I]] | + | [[Category: Kursula I]] |
| - | [[Category: Norledge, B V]] | + | [[Category: Norledge BV]] |
| - | [[Category: Salin, M]] | + | [[Category: Salin M]] |
| - | [[Category: Sampson, N S]] | + | [[Category: Sampson NS]] |
| - | [[Category: Sun, J]] | + | [[Category: Sun J]] |
| - | [[Category: Wierenga, R K]] | + | [[Category: Wierenga RK]] |
| - | [[Category: Flexible loop]]
| + | |
| - | [[Category: Hinge]]
| + | |
| - | [[Category: Isomerase]]
| + | |
| - | [[Category: Tim barrel]]
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| Structural highlights
Function
TPIS_CHICK
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kursula I, Salin M, Sun J, Norledge BV, Haapalainen AM, Sampson NS, Wierenga RK. Understanding protein lids: structural analysis of active hinge mutants in triosephosphate isomerase. Protein Eng Des Sel. 2004 Apr;17(4):375-82. Epub 2004 May 27. PMID:15166315 doi:10.1093/protein/gzh048
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