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Sulfurtransferase
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PDB id
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1h4m
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* Residue conservation analysis
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Enzyme class:
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E.C.2.8.1.1
- Thiosulfate sulfurtransferase.
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Reaction:
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Thiosulfate + cyanide = sulfite + thiocyanate
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Thiosulfate
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+
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cyanide
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=
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sulfite
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+
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thiocyanate
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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Gene Ontology (GO) functional annotation
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Cellular component
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cytoplasm
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1 term
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Biological process
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sulfate transport
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1 term
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Biochemical function
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transferase activity
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2 terms
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DOI no:
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Biol Chem
382:1245-1252
(2001)
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PubMed id:
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A persulfurated cysteine promotes active site reactivity in Azotobacter vinelandii Rhodanese.
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D.Bordo,
F.Forlani,
A.Spallarossa,
R.Colnaghi,
A.Carpen,
M.Bolognesi,
S.Pagani.
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ABSTRACT
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Active site reactivity and specificity of RhdA, a thiosulfate:cyanide
sulfurtransferase (rhodanese) from Azotobacter vinelandii, have been
investigated through ligand binding, site-directed mutagenesis, and X-ray
crystallographic techniques, in a combined approach. In native RhdA the active
site Cys230 is found persulfurated; fluorescence and sulfurtransferase activity
measurements show that phosphate anions interact with Cys230 persulfide sulfur
atom and modulate activity. Crystallographic analyses confirm that phosphate and
hypophosphite anions react with native RhdA, removing the persulfide sulfur atom
from the active site pocket. Considering that RhdA and the catalytic subunit of
Cdc25 phosphatases share a common three-dimensional fold as well as active site
Cys (catalytic) and Arg residues, two RhdA mutants carrying a single amino acid
insertion at the active site loop were designed and their phosphatase activity
tested. The crystallographic and functional results reported here show that
specific sulfurtransferase or phosphatase activities are strictly related to
precise tailoring of the catalytic loop structure in RhdA and Cdc25 phosphatase,
respectively.
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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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F.Cartini,
W.Remelli,
P.C.Dos Santos,
J.Papenbrock,
S.Pagani,
and
F.Forlani
(2011).
Mobilization of sulfane sulfur from cysteine desulfurases to the Azotobacter vinelandii sulfurtransferase RhdA.
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Amino Acids, 41,
141-150.
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P.Hänzelmann,
J.U.Dahl,
J.Kuper,
A.Urban,
U.Müller-Theissen,
S.Leimkühler,
and
H.Schindelin
(2009).
Crystal structure of YnjE from Escherichia coli, a sulfurtransferase with three rhodanese domains.
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Protein Sci, 18,
2480-2491.
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PDB codes:
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H.Cheng,
J.L.Donahue,
S.E.Battle,
W.K.Ray,
and
T.J.Larson
(2008).
Biochemical and Genetic Characterization of PspE and GlpE, Two Single-domain Sulfurtransferases of Escherichia coli.
|
| |
Open Microbiol J, 2,
18-28.
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L.Cavalca,
N.Guerrieri,
M.Colombo,
S.Pagani,
and
V.Andreoni
(2007).
Enzymatic and genetic profiles in environmental strains grown on polycyclic aromatic hydrocarbons.
|
| |
Antonie Van Leeuwenhoek, 91,
315-325.
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M.C.Giuliani,
P.Tron,
G.Leroy,
C.Aubert,
P.Tauc,
and
M.T.Giudici-Orticoni
(2007).
A new sulfurtransferase from the hyperthermophilic bacterium Aquifex aeolicus. Being single is not so simple when temperature gets high.
|
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FEBS J, 274,
4572-4587.
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D.Bisacchi,
Y.Zhou,
B.P.Rosen,
R.Mukhopadhyay,
and
D.Bordo
(2006).
Crystallization and preliminary crystallographic characterization of LmACR2, an arsenate/antimonate reductase from Leishmania major.
|
| |
Acta Crystallogr Sect F Struct Biol Cryst Commun, 62,
976-979.
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T.Tamura,
S.Yamamoto,
M.Takahata,
H.Sakaguchi,
H.Tanaka,
T.C.Stadtman,
and
K.Inagaki
(2004).
Selenophosphate synthetase genes from lung adenocarcinoma cells: Sps1 for recycling L-selenocysteine and Sps2 for selenite assimilation.
|
| |
Proc Natl Acad Sci U S A, 101,
16162-16167.
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A.Cereda,
F.Forlani,
S.Iametti,
R.Bernhardt,
P.Ferranti,
G.Picariello,
S.Pagani,
and
F.Bonomi
(2003).
Molecular recognition between Azotobacter vinelandii rhodanese and a sulfur acceptor protein.
|
| |
Biol Chem, 384,
1473-1481.
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S.Melino,
D.O.Cicero,
M.Orsale,
F.Forlani,
S.Pagani,
and
M.Paci
(2003).
Azotobacter vinelandii rhodanese: selenium loading and ion interaction studies.
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| |
Eur J Biochem, 270,
4208-4215.
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A.Spallarossa,
J.L.Donahue,
T.J.Larson,
M.Bolognesi,
and
D.Bordo
(2001).
Escherichia coli GlpE is a prototype sulfurtransferase for the single-domain rhodanese homology superfamily.
|
| |
Structure, 9,
1117-1125.
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PDB codes:
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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
codes are
shown on the right.
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Links
