1fux: Difference between revisions

← Older edit

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

OCA

@@ Line 1: / Line 1: @@
-{{Seed}}
-[[Image:1fux.png|left|200px]]
-<!--
+==CRYSTAL STRUCTURE OF E.COLI YBCL, A NEW MEMBER OF THE MAMMALIAN PEBP FAMILY==
-The line below this paragraph, containing "STRUCTURE_1fux", creates the "Structure Box" on the page.
+<StructureSection load='1fux' size='340' side='right'caption='[[1fux]], [[Resolution|resolution]] 1.81&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'>[[1fux]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FUX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FUX 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]] 1.81&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-{{STRUCTURE_1fux|  PDB=1fux  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fux FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fux OCA], [https://pdbe.org/1fux PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fux RCSB], [https://www.ebi.ac.uk/pdbsum/1fux PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fux ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/YBCL_ECOLI YBCL_ECOLI]
+== 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/fu/1fux_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=1fux ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+In rat and human cells, RKIP (previously known as PEBP) was characterized as an inhibitor of the MEK phosphorylation by Raf-1. In Escherichia coli, the genes ybhb and ybcl possibly encode two RKIP homologues while in the genomes of other bacteria and archaebacteria other homologous genes of RKIP have been found. The parallel between the cellular signaling mechanisms in eukaryotes and prokaryotes suggests that these bacterial proteins could be involved in the regulation of protein phosphorylation by kinases as well. We first showed that the proteins YBHB and YBCL were present in the cytoplasm and periplasm of E. coli, respectively, after which we determined their crystallographic structures. These structures verify that YBHB and YBCL belong to the same structural family as mammalian RKIP/PEBP proteins. The general fold and the anion binding site of these proteins are extremely well conserved between mammals and bacteria and suggest functional similarities. However, the bacterial proteins also exhibit some specific structural features, like a substrate binding pocket formed by the dimerization interface and the absence of cis peptide bonds. This structural variety should correspond to the recognition of multiple cellular partners.
-===CRYSTAL STRUCTURE OF E.COLI YBCL, A NEW MEMBER OF THE MAMMALIAN PEBP FAMILY===
+Crystal structures of YBHB and YBCL from Escherichia coli, two bacterial homologues to a Raf kinase inhibitor protein.,Serre L, Pereira de Jesus K, Zelwer C, Bureaud N, Schoentgen F, Benedetti H J Mol Biol. 2001 Jul 13;310(3):617-34. PMID:11439028<ref>PMID:11439028</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_11439028}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 1fux" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 11439028 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_11439028}}
+__TOC__
+</StructureSection>
-==About this Structure==
-FUX is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FUX OCA].
-==Reference==
-<ref group="xtra">PMID:11439028</ref><references group="xtra"/>
 [[Category: Escherichia coli]]
-[[Category: Benedetti, H.]]
+[[Category: Large Structures]]
-[[Category: Bureaud, N.]]
+[[Category: Benedetti H]]
-[[Category: Jesus, K Pereira de.]]
+[[Category: Bureaud N]]
-[[Category: Schoentgen, F.]]
+[[Category: Pereira de Jesus K]]
-[[Category: Serre, L.]]
+[[Category: Schoentgen F]]
-[[Category: Zelwer, C.]]
+[[Category: Serre L]]
-[[Category: Beta protein]]
+[[Category: Zelwer C]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 17:51:06 2009''