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Oxidoreductase
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PDB id
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2j6p
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Contents |
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* Residue conservation analysis
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PDB id:
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Oxidoreductase
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Title:
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Structure of as-sb reductase from leishmania major
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Structure:
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Sb(v)-as(v) reductase. Chain: a, b, c, d, e, f. Synonym: arsenate-antimonate reductase. Engineered: yes. Other_details: native protein
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Source:
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Leishmania major. Organism_taxid: 5664. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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2.15Å
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R-factor:
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0.193
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R-free:
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0.241
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Authors:
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D.Bisacchi,Y.Zhou,B.P.Rosen,R.Mukhopadhyay,D.Bordo
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Key ref:
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R.Mukhopadhyay
et al.
(2009).
Structural characterization of the As/Sb reductase LmACR2 from Leishmania major.
J Mol Biol,
386,
1229-1239.
PubMed id:
DOI:
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Date:
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02-Oct-06
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Release date:
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02-Oct-07
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PROCHECK
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Headers
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References
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Q6Q1Q5
(Q6Q1Q5_LEIMA) -
Sb(V)-As(V) reductase
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Seq:
Struc:
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127 a.a.
145 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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Gene Ontology (GO) functional annotation
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Cellular component
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intracellular
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1 term
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Biological process
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M phase of mitotic cell cycle
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3 terms
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Biochemical function
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protein tyrosine phosphatase activity
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1 term
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DOI no:
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J Mol Biol
386:1229-1239
(2009)
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PubMed id:
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Structural characterization of the As/Sb reductase LmACR2 from Leishmania major.
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R.Mukhopadhyay,
D.Bisacchi,
Y.Zhou,
A.Armirotti,
D.Bordo.
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ABSTRACT
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The arsenate/antimonate reductase LmACR2 has been recently identified in the
genome of Leishmania major. Besides displaying phosphatase activity in vitro,
this enzyme is able to reduce both As(V) and Sb(V) to their respective trivalent
forms and is involved in the activation of Pentostan, a drug containing Sb(V)
used in the treatment of leishmaniasis. LmACR2 displays sequence and functional
similarity with the arsenate reductase ScACR2 from Saccharomyces cerevisiae, and
both proteins are homologous to the catalytic domain of Cdc25 phosphatases,
which, in turn, belong to the rhodanese/Cdc25 phosphatase superfamily. In this
work, the three-dimensional structure of LmACR2 has been determined with
crystallographic methods and refined at 2.15 A resolution. The protein structure
maintains the overall rhodanese fold, but substantial modifications are observed
in secondary structure position and length. However, the conformation of the
active-site loop and the position of the catalytic residue Cys75 are unchanged
with respect to the Cdc25 phosphatases. From an evolutionary viewpoint, LmACR2
and the related arsenate reductases form, together with the known Cdc25
phosphatases, a well-defined subfamily of the rhodanese/Cdc25 phosphatase
superfamily, characterized by a 7-amino-acid-long active-site loop that is able
to selectively bind substrates containing phosphorous, arsenic, or antinomy. The
evolutionary tree obtained for these proteins shows that, besides the
active-site motif CE[F/Y]SXXR that characterizes Cdc25 phosphatase, the novel
CALSQ[Q/V]R motif is also conserved in sequences from fungi and plants. Similar
to Cdc25 phosphatase, these proteins are likely involved in cell cycle control.
The active-site composition of LmACR2 (CAQSLVR) does not belong to either group,
but gives to the enzyme a bifunctional activity of both phosphatase and As/Sb
reductase. The subtle dependence of substrate specificity on the amino acid
composition of the active-site loop displays the versatility of the ubiquitous
rhodanese domain.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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B.Szöör
(2010).
Trypanosomatid protein phosphatases.
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Mol Biochem Parasitol, 173,
53-63.
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W.Yang,
M.Pollard,
Y.Li-Beisson,
F.Beisson,
M.Feig,
and
J.Ohlrogge
(2010).
A distinct type of glycerol-3-phosphate acyltransferase with sn-2 preference and phosphatase activity producing 2-monoacylglycerol.
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Proc Natl Acad Sci U S A, 107,
12040-12045.
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E.Ordóñez,
K.Van Belle,
G.Roos,
S.De Galan,
M.Letek,
J.A.Gil,
L.Wyns,
L.M.Mateos,
and
J.Messens
(2009).
Arsenate reductase, mycothiol, and mycoredoxin concert thiol/disulfide exchange.
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J Biol Chem, 284,
15107-15116.
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H.K.Yeo,
and
J.Y.Lee
(2009).
Crystal structure of Saccharomyces cerevisiae Ygr203w, a homolog of single-domain rhodanese and Cdc25 phosphatase catalytic domain.
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Proteins, 76,
520-524.
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PDB code:
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
code is
shown on the right.
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Links
