1ok6: Difference between revisions

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-[[Image:1ok6.png|left|200px]]
-{{STRUCTURE_1ok6|  PDB=1ok6  |  SCENE=  }}
+==Orthorhombic crystal form of an Archaeal fructose 1,6-bisphosphate aldolase==
+<StructureSection load='1ok6' size='340' side='right'caption='[[1ok6]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1ok6]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermoproteus_tenax Thermoproteus tenax]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OK6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OK6 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]] 2.4&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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=1ok6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ok6 OCA], [https://pdbe.org/1ok6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ok6 RCSB], [https://www.ebi.ac.uk/pdbsum/1ok6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ok6 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/ok/1ok6_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=1ok6 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.
-===ORTHORHOMBIC CRYSTAL FORM OF AN ARCHAEAL FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE===
+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>
-{{ABSTRACT_PUBMED_12941964}}
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-==About this Structure==
+<div class="pdbe-citations 1ok6" style="background-color:#fffaf0;"></div>
-[[1ok6]] is a 10 chain structure of [[Aldolase]] with sequence from [http://en.wikipedia.org/wiki/Thermoproteus_tenax Thermoproteus tenax]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OK6 OCA].
 ==See Also==
-*[[Aldolase|Aldolase]]
+*[[Aldolase 3D structures|Aldolase 3D structures]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:012941964</ref><references group="xtra"/>
+__TOC__
-[[Category: Fructose-bisphosphate aldolase]]
+</StructureSection>
+[[Category: Large Structures]]
 [[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: Orthorhombic]]
-[[Category: Schiff base]]
-[[Category: Tim barrel]]