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PDBsum entry 1e20
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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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The X-Ray structure of the fmn-Binding protein athal3 provides the structural basis for the activity of a regulatory subunit involved in signal transduction.
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Authors
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A.Albert,
M.Martínez-Ripoll,
A.Espinosa-Ruiz,
L.Yenush,
F.A.Culiáñez-Macià,
R.Serrano.
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Ref.
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Structure, 2000,
8,
961-969.
[DOI no: ]
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PubMed id
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Abstract
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BACKGROUND: The Arabidopsis thaliana HAL3 gene product encodes for an
FMN-binding protein (AtHal3) that is related to plant growth and salt and
osmotic tolerance. AtHal3 shows sequence homology to ScHal3, a regulatory
subunit of the Saccharomyces cerevisae serine/threonine phosphatase PPz1. It has
been proposed that AtHal3 and ScHal3 have similar roles in cellular physiology,
as Arabidopsis transgenic plants that overexpress AtHal3 and yeast cells that
overexpress ScHal3 display similar phenotypes of improved salt tolerance. The
enzymatic activity of AtHal3 has not been investigated. However, the AtHal3
sequence is homologous to that of EpiD, a flavoprotein from Staphylococcus
epidermidis that recognizes a peptidic substrate and subsequently catalyzes the
alpha, beta-dehydrogenation of its C-terminal cysteine residue. RESULTS: The
X-ray structure of AtHal3 at 2 A resolution reveals that the biological unit is
a trimer. Each protomer adopts an alpha/beta Rossmann fold consisting of a
six-stranded parallel beta sheet flanked by two layers of alpha helices. The
FMN-binding site of AtHal3 contains all the structural requirements of the
flavoenzymes that catalyze dehydrogenation reactions. Comparison of the amino
acid sequences of AtHal3, ScHal3 and EpiD reveals that a significant number of
residues involved in trimer formation, the active site, and FMN binding are
conserved. This observation suggests that ScHal3 and EpiD might also be trimers,
having a similar structure and function to AtHal3. CONCLUSIONS: Structural
comparisons of AtHal3 with other FMN-binding proteins show that AtHal3 defines a
new subgroup of this protein family that is involved in signal transduction.
Analysis of the structure of AtHal3 indicates that this protein is designed to
interact with another cellular component and to subsequently catalyze the
alpha,beta-dehydrogenation of a peptidyl cysteine. Structural data from AtHal3,
together with physiological and biochemical information from ScHal3 and EpiD,
allow us to propose a model for the recognition and regulation of AtHal3/ScHal3
cellular partners.
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Figure 6.
Figure 6. The AtHal3 active site. (a) Stereoview detail of
the molecular surface using a probe of 1.4 Å [39]. A peptidyl
cysteine residue is modeled inside the cavity. (b) Proposed
mechanism for the a,b-dehydrogenation of a peptidyl cysteine
residue in the active site of AtHal3.
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The above figure is
reprinted
by permission from Cell Press:
Structure
(2000,
8,
961-969)
copyright 2000.
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