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PDBsum entry 1fux
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Unknown function
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PDB id
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1fux
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Crystal structures of ybhb and ybcl from escherichia coli, Two bacterial homologues to a raf kinase inhibitor protein.
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Authors
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L.Serre,
K.Pereira de jesus,
C.Zelwer,
N.Bureaud,
F.Schoentgen,
H.Bénédetti.
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Ref.
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J Mol Biol, 2001,
310,
617-634.
[DOI no: ]
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PubMed id
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Abstract
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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.
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Figure 6.
Figure 6. Superposition of the
binding sites of YBHB and YBCL.
Only residues with distinct confor-
mations have been represented by
ball-and-sticks. Magenta for YBHB
residues and green for YBCL resi-
dues. C
a
atoms of YBHB are
painted in pale pink and C
a
atoms
of YBCL in pale green
(Figure generated by RIBBONS).
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Figure 10.
Figure 10. Binding sites of
YBHB, YBCL, PEBP complexed
with phosphoryl-ethanolamine and
CEN. The structures are rep-
resented with the same orientation.
H-bonds are schematized by bro-
ken lines. Only conserved or water
molecules discussed are drawn.
(a) YBHB, (b) YBCL, (c) PEBP,
(d) CEN (Figures generated by
MOLSCRIPT and Raster3D).
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The above figures are
reprinted
by permission from Elsevier:
J Mol Biol
(2001,
310,
617-634)
copyright 2001.
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