2flf: Difference between revisions

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:2flf.jpg|left|200px]]<br /><applet load="2flf" size="350" color="white" frame="true" align="right" spinBox="true"
-caption="2flf, resolution 2.70&Aring;" />
-'''Crystal structure of l-fuculose-1-phosphate aldolase from Thermus Thermophilus HB8'''<br />
-==About this Structure==
+==Crystal structure of l-fuculose-1-phosphate aldolase from Thermus Thermophilus HB8==
-FLF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Active as [http://en.wikipedia.org/wiki/L-fuculose-phosphate_aldolase L-fuculose-phosphate aldolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.17 4.1.2.17] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FLF OCA].
+<StructureSection load='2flf' size='340' side='right'caption='[[2flf]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
-[[Category: L-fuculose-phosphate aldolase]]
+== Structural highlights ==
-[[Category: Single protein]]
+<table><tr><td colspan='2'>[[2flf]] is a 8 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=2FLF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FLF FirstGlance]. <br>
-[[Category: Thermus thermophilus]]
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
-[[Category: Jeyakanthan, J.]]
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2flf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2flf OCA], [https://pdbe.org/2flf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2flf RCSB], [https://www.ebi.ac.uk/pdbsum/2flf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2flf ProSAT], [https://www.topsan.org/Proteins/RSGI/2flf TOPSAN]</span></td></tr>
-[[Category: RSGI, RIKEN.Structural.Genomics/Proteomics.Initiative.]]
+</table>
-[[Category: Shiro, Y.]]
+== Function ==
-[[Category: Yokoyama, S.]]
+[https://www.uniprot.org/uniprot/Q5SHB9_THET8 Q5SHB9_THET8]
-[[Category: class ii aldolase]]
+== Evolutionary Conservation ==
-[[Category: fuculose phosphate]]
+[[Image:Consurf_key_small.gif|200px|right]]
-[[Category: metal binding]]
+Check<jmol>
-[[Category: national project on protein structural and functional analyses]]
+  <jmolCheckbox>
-[[Category: nppsfa]]
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fl/2flf_consurf.spt"</scriptWhenChecked>
-[[Category: riken structural genomics/proteomics initiative]]
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
-[[Category: rsgi]]
+    <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=2flf 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.
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 19:39:19 2008''
+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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2flf" 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]]
+[[Category: Yokoyama S]]