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{{STRUCTURE_3r1m|  PDB=3r1m  |  SCENE=  }}
===Strucure of bifunctional fructose 1,6-bisphosphate aldolase/phosphatase (aldolase form)===
{{ABSTRACT_PUBMED_21983966}}


==About this Structure==
==Structure of bifunctional fructose 1,6-bisphosphate aldolase/phosphatase (aldolase form)==
[[3r1m]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Sulfolobus_tokodaii Sulfolobus tokodaii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3R1M OCA].  
<StructureSection load='3r1m' size='340' side='right'caption='[[3r1m]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3r1m]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sulfurisphaera_tokodaii_str._7 Sulfurisphaera tokodaii str. 7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3R1M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3R1M 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]] 1.5&#8491;</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>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</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=3r1m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3r1m OCA], [https://pdbe.org/3r1m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3r1m RCSB], [https://www.ebi.ac.uk/pdbsum/3r1m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3r1m ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FBPAP_SULTO FBPAP_SULTO] Catalyzes two subsequent steps in gluconeogenesis: the aldol condensation of dihydroxyacetone phosphate (DHAP) and glyceraldehyde-3-phosphate (GA3P) to fructose-1,6-bisphosphate (FBP), and the dephosphorylation of FBP to fructose-6-phosphate (F6P).<ref>PMID:15274916</ref> <ref>PMID:20348906</ref> <ref>PMID:21983966</ref>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Enzymes catalyse specific reactions and are essential for maintaining life. Although some are referred to as being bifunctional, they consist of either two distinct catalytic domains or a single domain that displays promiscuous substrate specificity. Thus, one enzyme active site is generally responsible for one biochemical reaction. In contrast to this conventional concept, archaeal fructose-1,6-bisphosphate (FBP) aldolase/phosphatase (FBPA/P) consists of a single catalytic domain, but catalyses two chemically distinct reactions of gluconeogenesis: (1) the reversible aldol condensation of dihydroxyacetone phosphate (DHAP) and glyceraldehyde-3-phosphate (GA3P) to FBP; (2) the dephosphorylation of FBP to fructose-6-phosphate (F6P). Thus, FBPA/P is fundamentally different from ordinary enzymes whose active sites are responsible for a specific reaction. However, the molecular mechanism by which FBPA/P achieves its unusual bifunctionality remains unknown. Here we report the crystal structure of FBPA/P at 1.5-A resolution in the aldolase form, where a critical lysine residue forms a Schiff base with DHAP. A structural comparison of the aldolase form with a previously determined phosphatase form revealed a dramatic conformational change in the active site, demonstrating that FBPA/P metamorphoses its active-site architecture to exhibit dual activities. Thus, our findings expand the conventional concept that one enzyme catalyses one biochemical reaction.


==See Also==
Structural basis for the bifunctionality of fructose-1,6-bisphosphate aldolase/phosphatase.,Fushinobu S, Nishimasu H, Hattori D, Song HJ, Wakagi T Nature. 2011 Oct 9;478(7370):538-41. doi: 10.1038/nature10457. PMID:21983966<ref>PMID:21983966</ref>
*[[Suggestions for new articles|Suggestions for new articles]]


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
<ref group="xtra">PMID:021983966</ref><references group="xtra"/>
</div>
[[Category: Sulfolobus tokodaii]]
<div class="pdbe-citations 3r1m" style="background-color:#fffaf0;"></div>
[[Category: Fushinobu, S.]]
== References ==
[[Category: Hattori, D.]]
<references/>
[[Category: Nishimasu, H.]]
__TOC__
[[Category: Song, H J.]]
</StructureSection>
[[Category: Wakagi, T.]]
[[Category: Large Structures]]
[[Category: 6-bisphosphatase-like fold]]
[[Category: Sulfurisphaera tokodaii str. 7]]
[[Category: Hydrolase/aldolase]]
[[Category: Fushinobu S]]
[[Category: Metal binding protein]]
[[Category: Hattori D]]
[[Category: Mg binding]]
[[Category: Nishimasu H]]
[[Category: Sulfolobus fructose-1]]
[[Category: Song H-J]]
[[Category: Wakagi T]]
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