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1ojx
From Proteopedia
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| - | [[Image:1ojx.png|left|200px]] | ||
| - | + | ==Crystal structure of an Archaeal fructose 1,6-bisphosphate aldolase== | |
| + | <StructureSection load='1ojx' size='340' side='right'caption='[[1ojx]], [[Resolution|resolution]] 1.90Å' 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]] 1.9Å</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. | ||
| - | + | 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> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1ojx" style="background-color:#fffaf0;"></div> | |
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==See Also== | ==See Also== | ||
| - | *[[Aldolase|Aldolase]] | + | *[[Aldolase 3D structures|Aldolase 3D structures]] |
| - | + | == References == | |
| - | == | + | <references/> |
| - | < | + | __TOC__ |
| - | [[Category: | + | </StructureSection> |
| + | [[Category: Large Structures]] | ||
[[Category: RCSB PDB Molecule of the Month]] | [[Category: RCSB PDB Molecule of the Month]] | ||
[[Category: The Glycolytic Enzymes]] | [[Category: The Glycolytic Enzymes]] | ||
[[Category: Thermoproteus tenax]] | [[Category: Thermoproteus tenax]] | ||
| - | [[Category: Hensel | + | [[Category: Hensel R]] |
| - | [[Category: Lorentzen | + | [[Category: Lorentzen E]] |
| - | [[Category: Pohl | + | [[Category: Pohl E]] |
| - | [[Category: Siebers | + | [[Category: Siebers B]] |
| - | [[Category: Stark | + | [[Category: Stark A]] |
| - | [[Category: Zwart | + | [[Category: Zwart P]] |
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Current revision
Crystal structure of an Archaeal fructose 1,6-bisphosphate aldolase
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