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* Residue conservation analysis
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Enzyme class:
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E.C.3.5.4.1
- Cytosine deaminase.
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Reaction:
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Cytosine + H2O = uracil + NH3
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Cytosine
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+
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H(2)O
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=
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uracil
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+
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NH(3)
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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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2 terms
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Biological process
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pyrimidine salvage
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3 terms
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Biochemical function
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catalytic activity
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7 terms
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DOI no:
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Acta Crystallogr D Biol Crystallogr
60:601-605
(2004)
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PubMed id:
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Microseed matrix screening to improve crystals of yeast cytosine deaminase.
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G.C.Ireton,
B.L.Stoddard.
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ABSTRACT
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A crystallization strategy termed 'microseed matrix screening' is described
where the optimal conditions for nucleation versus extended lattice growth are
not compatible. This method is an extension of conventional seeding techniques
in which microseeds from the nucleation step are systematically seeded into new
conditions where all components of the drop are allowed to vary to screen for
subsequent growth of well ordered specimens. The structure of a crystal form of
yeast cytosine deaminase produced by streak-seeding using a single condition for
both nucleation and growth is compared with the structure of a related crystal
form produced by separating nucleation and growth conditions. The resulting
structural comparison demonstrates that differential chelation patterns of
cations by acidic surface residues of proteins within crystal lattice contacts
is a critical parameter of crystal nucleation and growth.
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Selected figure(s)
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Figure 3.
Figure 3 Calcium-mediated lattice contacts in crystal form II
and the corresponding region in initial crystal form I. (a) A
bound calcium ion is coordinated by surface side chains from
three separate enzyme subunits: Glu75A and Gln150B from a
physiological dimer and Glu128B' (green) from a subunit of a
neighboring asymmetric unit. (b) In the presence of sodium in
the initial crystallization condition (form I) no bound cation
is visible and the corresponding side chains are further apart.
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The above figure is
reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(2004,
60,
601-605)
copyright 2004.
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Figure was
selected
by an automated process.
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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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A.G.Villaseñor,
A.Wong,
A.Shao,
A.Garg,
A.Kuglstatter,
and
S.F.Harris
(2010).
Acoustic matrix microseeding: improving protein crystal growth with minimal chemical bias.
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Acta Crystallogr D Biol Crystallogr, 66,
568-576.
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G.Obmolova,
T.J.Malia,
A.Teplyakov,
R.Sweet,
and
G.L.Gilliland
(2010).
Promoting crystallization of antibody-antigen complexes via microseed matrix screening.
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Acta Crystallogr D Biol Crystallogr, 66,
927-933.
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J.M.Kallio,
N.Hakulinen,
J.P.Kallio,
M.H.Niemi,
S.Kärkkäinen,
and
J.Rouvinen
(2009).
The contribution of polystyrene nanospheres towards the crystallization of proteins.
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PLoS ONE, 4,
e4198.
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B.A.Manjasetty,
A.P.Turnbull,
S.Panjikar,
K.Büssow,
and
M.R.Chance
(2008).
Automated technologies and novel techniques to accelerate protein crystallography for structural genomics.
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Proteomics, 8,
612-625.
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T.S.Walter,
E.J.Mancini,
J.Kadlec,
S.C.Graham,
R.Assenberg,
J.Ren,
S.Sainsbury,
R.J.Owens,
D.I.Stuart,
J.M.Grimes,
and
K.Harlos
(2008).
Semi-automated microseeding of nanolitre crystallization experiments.
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Acta Crystallogr Sect F Struct Biol Cryst Commun, 64,
14-18.
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J.R.Thompson,
Z.C.Ryan,
J.L.Salisbury,
and
R.Kumar
(2006).
The structure of the human centrin 2-xeroderma pigmentosum group C protein complex.
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J Biol Chem, 281,
18746-18752.
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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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