1fux: Difference between revisions
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<StructureSection load='1fux' size='340' side='right'caption='[[1fux]], [[Resolution|resolution]] 1.81Å' scene=''> | <StructureSection load='1fux' size='340' side='right'caption='[[1fux]], [[Resolution|resolution]] 1.81Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1fux]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <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> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.81Å</td></tr> | ||
<tr id=' | <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> | ||
<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> | <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> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/YBCL_ECOLI YBCL_ECOLI] | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Escherichia coli]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Benedetti | [[Category: Benedetti H]] | ||
[[Category: Bureaud | [[Category: Bureaud N]] | ||
[[Category: Jesus | [[Category: Pereira de Jesus K]] | ||
[[Category: Schoentgen | [[Category: Schoentgen F]] | ||
[[Category: Serre | [[Category: Serre L]] | ||
[[Category: Zelwer | [[Category: Zelwer C]] | ||
Revision as of 09:05, 9 August 2023
CRYSTAL STRUCTURE OF E.COLI YBCL, A NEW MEMBER OF THE MAMMALIAN PEBP FAMILYCRYSTAL STRUCTURE OF E.COLI YBCL, A NEW MEMBER OF THE MAMMALIAN PEBP FAMILY
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedIn 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 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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