1fux: Difference between revisions

Revision as of 13:42, 21 February 2008

CRYSTAL STRUCTURE OF E.COLI YBCL, A NEW MEMBER OF THE MAMMALIAN PEBP FAMILY

OverviewOverview

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.

About this StructureAbout this Structure

1FUX is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

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

Page seeded by OCA on Thu Feb 21 12:42:53 2008

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OCA

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-[[Image:1fux.gif|left|200px]]<br /><applet load="1fux" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1fux.gif|left|200px]]<br /><applet load="1fux" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1fux, resolution 1.81&Aring;" />
 '''CRYSTAL STRUCTURE OF E.COLI YBCL, A NEW MEMBER OF THE MAMMALIAN PEBP FAMILY'''<br />
 ==Overview==
-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.
+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.
 ==About this Structure==
-FUX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FUX OCA].
+FUX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence 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==
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 [[Category: Benedetti, H.]]
 [[Category: Bureaud, N.]]
-[[Category: Jesus, K.Pereira.de.]]
+[[Category: Jesus, K Pereira de.]]
 [[Category: Schoentgen, F.]]
 [[Category: Serre, L.]]
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 [[Category: beta protein]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:19:14 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:42:53 2008''