1spq: Difference between revisions

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OCA

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-[[Image:1spq.gif|left|200px]]<br /><applet load="1spq" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1spq, resolution 2.16&Aring;" />
-'''Understanding protein lids: Structural analysis of active hinge mutants in triosephosphate isomerase'''<br />
-==Overview==
+==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, 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.
+<StructureSection load='1spq' size='340' side='right'caption='[[1spq]], [[Resolution|resolution]] 2.16&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1spq]] 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=1SPQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SPQ 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]] 2.16&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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=1spq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1spq OCA], [https://pdbe.org/1spq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1spq RCSB], [https://www.ebi.ac.uk/pdbsum/1spq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1spq 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/sp/1spq_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=1spq 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.
-==About this Structure==
+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>
-SPQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with PEG 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=1SPQ OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15166315 15166315]
+</div>
+<div class="pdbe-citations 1spq" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Triose phosphate isomerase 3D structures|Triose phosphate isomerase 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Gallus gallus]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Triose-phosphate isomerase]]
+[[Category: Haapalainen AM]]
-[[Category: Haapalainen, A.M.]]
+[[Category: Kursula I]]
-[[Category: Kursula, I.]]
+[[Category: Norledge BV]]
-[[Category: Norledge, B.V.]]
+[[Category: Salin M]]
-[[Category: Salin, M.]]
+[[Category: Sampson NS]]
-[[Category: Sampson, N.S.]]
+[[Category: Sun J]]
-[[Category: Sun, J.]]
+[[Category: Wierenga RK]]
-[[Category: Wierenga, R.K.]]
-[[Category: PEG]]
-[[Category: archae]]
-[[Category: evolution]]
-[[Category: flexible loop-6]]
-[[Category: n-hinge]]
-[[Category: tim]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 02:33:05 2007''