This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
2fk5
From Proteopedia
(Difference between revisions)
| (18 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | [[Image:2fk5.jpg|left|200px]]<br /><applet load="2fk5" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2fk5, resolution 1.90Å" /> | ||
| - | '''Crystal structure of l-fuculose-1-phosphate aldolase from Thermus thermophilus HB8'''<br /> | ||
| - | == | + | ==Crystal structure of l-fuculose-1-phosphate aldolase from Thermus thermophilus HB8== |
| - | + | <StructureSection load='2fk5' size='340' side='right'caption='[[2fk5]], [[Resolution|resolution]] 1.90Å' scene=''> | |
| - | [ | + | == Structural highlights == |
| - | [ | + | <table><tr><td colspan='2'>[[2fk5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FK5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FK5 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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=2fk5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fk5 OCA], [https://pdbe.org/2fk5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fk5 RCSB], [https://www.ebi.ac.uk/pdbsum/2fk5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fk5 ProSAT], [https://www.topsan.org/Proteins/RSGI/2fk5 TOPSAN]</span></td></tr> |
| - | [ | + | </table> |
| - | + | == Function == | |
| - | [[ | + | [https://www.uniprot.org/uniprot/Q5SHB9_THET8 Q5SHB9_THET8] |
| - | + | == 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/fk/2fk5_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=2fk5 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Fuculose phosphate aldolase catalyzes the reversible cleavage of L-fuculose-1-phosphate to dihydroxyacetone phosphate and L-lactaldehyde. The protein from Thermus thermophilus HB8 is a biological tetramer with a subunit molecular weight of 21 591 Da. Purified FucA has been crystallized using sitting-drop vapour-diffusion and microbatch techniques at 293 K. The crystals belong to space group P4, with unit-cell parameters a = b = 100.94, c = 45.87 A. The presence of a dimer of the enzyme in the asymmetric unit was estimated to give a Matthews coefficient (VM) of 2.7 A3 Da(-1) and a solvent content of 54.2%(v/v). Three-wavelength diffraction MAD data were collected to 2.3 A from zinc-containing crystals. Native diffraction data to 1.9 A resolution have been collected using synchrotron radiation at SPring-8. | ||
| - | + | Purification, crystallization and preliminary X-ray crystallographic study of the L-fuculose-1-phosphate aldolase (FucA) from Thermus thermophilus HB8.,Jeyakanthan J, Taka J, Kikuchi A, Kuroishi C, Yutani K, Shiro Y Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Dec 1;61(Pt, 12):1075-7. Epub 2005 Nov 24. PMID:16511238<ref>PMID:16511238</ref> | |
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 2fk5" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Aldolase 3D structures|Aldolase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Thermus thermophilus HB8]] | ||
| + | [[Category: Jeyakanthan J]] | ||
| + | [[Category: Shiro Y]] | ||
Current revision
Crystal structure of l-fuculose-1-phosphate aldolase from Thermus thermophilus HB8
| |||||||||||
