3t2c: Difference between revisions
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==Fructose-1,6-bisphosphate aldolase/phosphatase from Thermoproteus neutrophilus, DHAP-bound form== | ==Fructose-1,6-bisphosphate aldolase/phosphatase from Thermoproteus neutrophilus, DHAP-bound form== | ||
<StructureSection load='3t2c' size='340' side='right' caption='[[3t2c]], [[Resolution|resolution]] 1.30Å' scene=''> | <StructureSection load='3t2c' size='340' side='right' caption='[[3t2c]], [[Resolution|resolution]] 1.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3t2c]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3t2c]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrnv Pyrnv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3T2C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3T2C FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=13P:1,3-DIHYDROXYACETONEPHOSPHATE'>13P</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=13P:1,3-DIHYDROXYACETONEPHOSPHATE'>13P</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3t2b|3t2b]], [[3t2d|3t2d]], [[3t2e|3t2e]], [[3t2f|3t2f]], [[3t2g|3t2g]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3t2b|3t2b]], [[3t2d|3t2d]], [[3t2e|3t2e]], [[3t2f|3t2f]], [[3t2g|3t2g]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Tneu_0133 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id= | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Tneu_0133 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=444157 PYRNV])</td></tr> | ||
<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=3t2c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t2c OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3t2c RCSB], [http://www.ebi.ac.uk/pdbsum/3t2c PDBsum]</span></td></tr> | <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=3t2c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t2c OCA], [http://pdbe.org/3t2c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3t2c RCSB], [http://www.ebi.ac.uk/pdbsum/3t2c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3t2c ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 3t2c" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Pyrnv]] | ||
[[Category: Du, J]] | [[Category: Du, J]] | ||
[[Category: Einsle, O]] | [[Category: Einsle, O]] | ||
Revision as of 02:28, 5 August 2016
Fructose-1,6-bisphosphate aldolase/phosphatase from Thermoproteus neutrophilus, DHAP-bound formFructose-1,6-bisphosphate aldolase/phosphatase from Thermoproteus neutrophilus, DHAP-bound form
Structural highlights
Publication Abstract from PubMedFructose-1,6-bisphosphate (FBP) aldolase/phosphatase is a bifunctional, thermostable enzyme that catalyses two subsequent steps in gluconeogenesis in most archaea and in deeply branching bacterial lineages. It mediates the aldol condensation of heat-labile dihydroxyacetone phosphate (DHAP) and glyceraldehyde-3-phosphate (GAP) to FBP, as well as the subsequent, irreversible hydrolysis of the product to yield the stable fructose-6-phosphate (F6P) and inorganic phosphate; no reaction intermediates are released. Here we present a series of structural snapshots of the reaction that reveal a substantial remodelling of the active site through the movement of loop regions that create different catalytic functionalities at the same location. We have solved the three-dimensional structures of FBP aldolase/phosphatase from thermophilic Thermoproteus neutrophilus in a ligand-free state as well as in complex with the substrates DHAP and FBP and the product F6P to resolutions up to 1.3 A. In conjunction with mutagenesis data, this pinpoints the residues required for the two reaction steps and shows that the sequential binding of additional Mg(2+) cations reversibly facilitates the reaction. FBP aldolase/phosphatase is an ancestral gluconeogenic enzyme optimized for high ambient temperatures, and our work resolves how consecutive structural rearrangements reorganize the catalytic centre of the protein to carry out two canonical reactions in a very non-canonical type of bifunctionality. Active-site remodelling in the bifunctional fructose-1,6-bisphosphate aldolase/phosphatase.,Du J, Say RF, Lu W, Fuchs G, Einsle O Nature. 2011 Oct 9. doi: 10.1038/nature10458. PMID:21983965[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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