2ftk: Difference between revisions

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-{{Seed}}
-[[Image:2ftk.png|left|200px]]
-<!--
+==berylloflouride Spo0F complex with Spo0B==
-The line below this paragraph, containing "STRUCTURE_2ftk", creates the "Structure Box" on the page.
+<StructureSection load='2ftk' size='340' side='right'caption='[[2ftk]], [[Resolution|resolution]] 3.05&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[2ftk]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FTK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FTK FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.05&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BFD:ASPARTATE+BERYLLIUM+TRIFLUORIDE'>BFD</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-{{STRUCTURE_2ftk|  PDB=2ftk  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ftk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ftk OCA], [https://pdbe.org/2ftk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ftk RCSB], [https://www.ebi.ac.uk/pdbsum/2ftk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ftk ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/SP0B_BACSU SP0B_BACSU] Key element in the phosphorelay regulating sporulation initiation. Acts on spo0A. Mediates reversible phosphoryl transfer from spo0F to spo0A.
+== 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/ft/2ftk_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2ftk ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+A number of regulatory circuits in biological systems function through the exchange of phosphoryl groups from one protein to another. Spo0F and Spo0B are components of a phosphorelay that control sporulation in the bacterium Bacillus subtilis through the exchange of a phosphoryl group. Using beryllofluoride as a mimic for phosphorylation, we trapped the interaction of the phosphorylated Spo0F with Spo0B in the crystal lattice. The transition state of phosphoryl transfer continues to be a highly debated issue, as to whether it is associative or dissociative in nature. The geometry of Spo0F binding to Spo0B favors an associative mechanism for phosphoryl transfer. In order to visualize the autophosphorylation of the histidine kinase, KinA, and the subsequent phosphoryl transfer to Spo0F, we generated in silico models representing these reaction steps.
-===berylloflouride Spo0F complex with Spo0B===
+The crystal structure of beryllofluoride Spo0F in complex with the phosphotransferase Spo0B represents a phosphotransfer pretransition state.,Varughese KI, Tsigelny I, Zhao H J Bacteriol. 2006 Jul;188(13):4970-7. PMID:16788205<ref>PMID:16788205</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2ftk" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_16788205}}, adds the Publication Abstract to the page
+*[[Phosphotransferase 3D structures|Phosphotransferase 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 16788205 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_16788205}}
+__TOC__
+</StructureSection>
-==About this Structure==
-FTK is a 8 chains structure of sequences from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FTK OCA].
-==Reference==
-<ref group="xtra">PMID:16788205</ref><references group="xtra"/>
 [[Category: Bacillus subtilis]]
-[[Category: Varughese, K I.]]
+[[Category: Large Structures]]
-[[Category: Spo0b phosphorelay]]
+[[Category: Varughese KI]]
-[[Category: Spo0f]]
-[[Category: Sporulation]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 23:12:42 2009''