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[[Image:1ojx.gif|left|200px]]
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{{STRUCTURE_1ojx|  PDB=1ojx  |  SCENE=  }}
'''CRYSTAL STRUCTURE OF AN ARCHAEAL FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE'''


==Crystal structure of an Archaeal fructose 1,6-bisphosphate aldolase==
<StructureSection load='1ojx' size='340' side='right'caption='[[1ojx]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1ojx]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermoproteus_tenax Thermoproteus tenax]. The February 2004 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''The Glycolytic Enzymes''  by David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2004_2 10.2210/rcsb_pdb/mom_2004_2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OJX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OJX 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]] 1.9&#8491;</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=1ojx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ojx OCA], [https://pdbe.org/1ojx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ojx RCSB], [https://www.ebi.ac.uk/pdbsum/1ojx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ojx ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ALF1_THETK ALF1_THETK] Catalyzes the reversible cleavage of fructose 1,6-bisphosphate (FBP) to glyceraldehyde 3-phosphate (GAP) and dihydroxyacetone phosphate (DHAP).
== 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/oj/1ojx_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=1ojx ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Fructose-1,6-bisphosphate aldolase (FBPA) catalyzes the reversible cleavage of fructose 1,6-bisphosphate to glyceraldehyde 3-phosphate and dihydroxyacetone phosphate in the glycolytic pathway. FBPAs from archaeal organisms have recently been identified and characterized as a divergent family of proteins. Here, we report the first crystal structure of an archaeal FBPA at 1.9-A resolution. The structure of this 280-kDa protein complex was determined using single wavelength anomalous dispersion followed by 10-fold non-crystallographic symmetry averaging and refined to an R-factor of 14.9% (Rfree 17.9%). The protein forms a dimer of pentamers, consisting of subunits adopting the ubiquitous (betaalpha)8 barrel fold. Additionally, a crystal structure of the archaeal FBPA covalently bound to dihydroxyacetone phosphate was solved at 2.1-A resolution. Comparison of the active site residues with those of classical FBPAs, which share no significant sequence identity but display the same overall fold, reveals a common ancestry between these two families of FBPAs. Structural comparisons, furthermore, establish an evolutionary link to the triosephosphate isomerases, a superfamily hitherto considered independent from the superfamily of aldolases.


==Overview==
Crystal structure of an archaeal class I aldolase and the evolution of (betaalpha)8 barrel proteins.,Lorentzen E, Pohl E, Zwart P, Stark A, Russell RB, Knura T, Hensel R, Siebers B J Biol Chem. 2003 Nov 21;278(47):47253-60. Epub 2003 Aug 26. PMID:12941964<ref>PMID:12941964</ref>
Fructose-1,6-bisphosphate aldolase (FBPA) catalyzes the reversible cleavage of fructose 1,6-bisphosphate to glyceraldehyde 3-phosphate and dihydroxyacetone phosphate in the glycolytic pathway. FBPAs from archaeal organisms have recently been identified and characterized as a divergent family of proteins. Here, we report the first crystal structure of an archaeal FBPA at 1.9-A resolution. The structure of this 280-kDa protein complex was determined using single wavelength anomalous dispersion followed by 10-fold non-crystallographic symmetry averaging and refined to an R-factor of 14.9% (Rfree 17.9%). The protein forms a dimer of pentamers, consisting of subunits adopting the ubiquitous (betaalpha)8 barrel fold. Additionally, a crystal structure of the archaeal FBPA covalently bound to dihydroxyacetone phosphate was solved at 2.1-A resolution. Comparison of the active site residues with those of classical FBPAs, which share no significant sequence identity but display the same overall fold, reveals a common ancestry between these two families of FBPAs. Structural comparisons, furthermore, establish an evolutionary link to the triosephosphate isomerases, a superfamily hitherto considered independent from the superfamily of aldolases.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1OJX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermoproteus_tenax Thermoproteus tenax]. The following page contains interesting information on the relation of 1OJX with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb50_1.html The Glycolytic Enzymes]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OJX OCA].
</div>
<div class="pdbe-citations 1ojx" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Crystal structure of an archaeal class I aldolase and the evolution of (betaalpha)8 barrel proteins., Lorentzen E, Pohl E, Zwart P, Stark A, Russell RB, Knura T, Hensel R, Siebers B, J Biol Chem. 2003 Nov 21;278(47):47253-60. Epub 2003 Aug 26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12941964 12941964]
*[[Aldolase 3D structures|Aldolase 3D structures]]
[[Category: Fructose-bisphosphate aldolase]]
== References ==
[[Category: Single protein]]
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: RCSB PDB Molecule of the Month]]
[[Category: The Glycolytic Enzymes]]
[[Category: The Glycolytic Enzymes]]
[[Category: Thermoproteus tenax]]
[[Category: Thermoproteus tenax]]
[[Category: Hensel, R.]]
[[Category: Hensel R]]
[[Category: Lorentzen, E.]]
[[Category: Lorentzen E]]
[[Category: Pohl, E.]]
[[Category: Pohl E]]
[[Category: Siebers, B.]]
[[Category: Siebers B]]
[[Category: Stark, A.]]
[[Category: Stark A]]
[[Category: Zwart, P.]]
[[Category: Zwart P]]
[[Category: 6-bisphosphate]]
[[Category: Aldolase]]
[[Category: Archaeal]]
[[Category: Fructose 1]]
[[Category: Glycolytic]]
[[Category: Lyase]]
[[Category: Tim barrel]]
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Retrieved from "https://proteopedia.org/1ojx"