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2fjk
From Proteopedia
(Difference between revisions)
(New page: 200px<br /><applet load="2fjk" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fjk, resolution 2.2Å" /> '''Crystal structure of ...) |
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| - | [[Image:2fjk.gif|left|200px]]<br /><applet load="2fjk" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2fjk, resolution 2.2Å" /> | ||
| - | '''Crystal structure of Fructose-1,6-Bisphosphate Aldolase in Thermus caldophilus'''<br /> | ||
| - | == | + | ==Crystal structure of Fructose-1,6-Bisphosphate Aldolase in Thermus caldophilus== |
| - | It was recently established that fructose-1,6-bisphosphate (FBP) aldolase | + | <StructureSection load='2fjk' size='340' side='right'caption='[[2fjk]], [[Resolution|resolution]] 2.20Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2fjk]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/"thermus_caldophilus"_taguchi_et_al._1983 "thermus caldophilus" taguchi et al. 1983]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FJK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FJK FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=13P:1,3-DIHYDROXYACETONEPHOSPHATE'>13P</scene></td></tr> | ||
| + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Fructose-bisphosphate_aldolase Fructose-bisphosphate aldolase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.13 4.1.2.13] </span></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=2fjk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fjk OCA], [https://pdbe.org/2fjk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fjk RCSB], [https://www.ebi.ac.uk/pdbsum/2fjk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fjk ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == 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/fj/2fjk_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=2fjk ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | It was recently established that fructose-1,6-bisphosphate (FBP) aldolase (FBA) and tagatose-1,6-bisphosphate (TBP) aldolase (TBA), two class II aldolases, are highly specific for the diastereoselective synthesis of FBP and TBP from glyceraldehyde-3-phosphate (G3P) and dihydroxyacetone phosphate (DHAP), respectively. In this paper, we report on a FBA from the thermophile Thermus caldophilus GK24 (Tca) that produces both FBP and TBP from C(3) substrates. Moreover, the FBP:TBP ratio could be adjusted by manipulating the concentrations of G3P and DHAP. This is the first native FBA known to show dual diastereoselectivity among the FBAs and TBAs characterized thus far. To explain the behavior of this enzyme, the X-ray crystal structure of the Tca FBA in complex with DHAP was determined at 2.2A resolution. It appears that as a result of alteration of five G3P binding residues, the substrate binding cavity of Tca FBA has a greater volume than those in the Escherichia coli FBA-phosphoglycolohydroxamate (PGH) and TBA-PGH complexes. We suggest that this steric difference underlies the difference in the diastereoselectivities of these class II aldolases. | ||
| - | + | Stereoselectivity of fructose-1,6-bisphosphate aldolase in Thermus caldophilus.,Lee JH, Bae J, Kim D, Choi Y, Im YJ, Koh S, Kim JS, Kim MK, Kang GB, Hong SI, Lee DS, Eom SH Biochem Biophys Res Commun. 2006 Sep 1;347(3):616-25. Epub 2006 Jul 5. PMID:16843441<ref>PMID:16843441</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 2fjk" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[Aldolase 3D structures|Aldolase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Thermus caldophilus taguchi et al. 1983]] | ||
| + | [[Category: Fructose-bisphosphate aldolase]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Eom, S H]] | ||
| + | [[Category: Im, Y J]] | ||
| + | [[Category: Kang, G B]] | ||
| + | [[Category: Kim, M K]] | ||
| + | [[Category: Lee, J H]] | ||
| + | [[Category: Rho, S H]] | ||
| + | [[Category: Beta-alpha-barrel]] | ||
| + | [[Category: Lyase]] | ||
Current revision
Crystal structure of Fructose-1,6-Bisphosphate Aldolase in Thermus caldophilus
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