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PDBsum entry 2zyt
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Contents |
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* Residue conservation analysis
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PDB id:
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Transferase
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Title:
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Crystal structure of mouse cytosolic sulfotransferase msult1d1 complex with paps
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Structure:
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Tyrosine-ester sulfotransferase. Chain: x. Fragment: residues 1-295. Synonym: cytosolic sulfotransferase, msult1d1. Engineered: yes
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Source:
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Mus musculus. Mouse. Organism_taxid: 10090. Gene: sult1d1. Expressed in: escherichia coli. Expression_system_taxid: 511693.
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Resolution:
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1.55Å
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R-factor:
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0.192
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R-free:
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0.210
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Authors:
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T.Teramoto,Y.Sakakibara,M.-C.Liu,M.Suiko,M.Kimura,Y.Kakuta
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Key ref:
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T.Teramoto
et al.
(2009).
Snapshot of a Michaelis complex in a sulfuryl transfer reaction: Crystal structure of a mouse sulfotransferase, mSULT1D1, complexed with donor substrate and accepter substrate.
Biochem Biophys Res Commun,
383,
83-87.
PubMed id:
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Date:
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29-Jan-09
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Release date:
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21-Apr-09
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PROCHECK
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Headers
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References
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Q3UZZ6
(ST1D1_MOUSE) -
Sulfotransferase 1 family member D1 from Mus musculus
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Seq:
Struc:
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295 a.a.
291 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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Biochem Biophys Res Commun
383:83-87
(2009)
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PubMed id:
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Snapshot of a Michaelis complex in a sulfuryl transfer reaction: Crystal structure of a mouse sulfotransferase, mSULT1D1, complexed with donor substrate and accepter substrate.
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T.Teramoto,
Y.Sakakibara,
M.C.Liu,
M.Suiko,
M.Kimura,
Y.Kakuta.
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ABSTRACT
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We report the crystal structure of mouse sulfotransferase, mSULT1D1, complexed
with donor substrate 3'-phosphoadenosine 5'-phosphosulfate and accepter
substrate p-nitrophenol. The structure is the first report of the native
Michaelis complex of sulfotransferase. In the structure, three proposed
catalytic residues (Lys48, Lys106, and His108) were in proper positions for
engaging in the sulfuryl transfer reaction. The data strongly support that the
sulfuryl transfer reaction proceeds through an S(N)2-like in-line displacement
mechanism.
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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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M.M.Hossain,
Y.Moriizumi,
S.Tanaka,
M.Kimura,
and
Y.Kakuta
(2011).
Molecular cloning, expression, and functional analysis of a predicted sulfotransferase STF9 from Mycobacterium avium.
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Mol Cell Biochem,
350,
155-162.
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G.Malojcić,
and
R.Glockshuber
(2010).
The PAPS-independent aryl sulfotransferase and the alternative disulfide bond formation system in pathogenic bacteria.
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Antioxid Redox Signal,
13,
1247-1259.
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L.M.Danan,
Z.Yu,
P.J.Ludden,
W.Jia,
K.L.Moore,
and
J.A.Leary
(2010).
Catalytic mechanism of Golgi-resident human tyrosylprotein sulfotransferase-2: a mass spectrometry approach.
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J Am Soc Mass Spectrom,
21,
1633-1642.
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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.
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Links
