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* Residue conservation analysis
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Enzyme class:
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E.C.2.7.7.72
- Cca tRNA nucleotidyltransferase.
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Reaction:
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A tRNA precursor + 2 CTP + ATP = a tRNA with a 3' CCA end + 3 diphosphate
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tRNA precursor
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+
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2
×
CTP
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+
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ATP
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=
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tRNA with a 3' CCA end
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+
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3
×
diphosphate
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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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Biological process
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RNA repair
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4 terms
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Biochemical function
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nucleotide binding
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8 terms
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DOI no:
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Embo J
22:5918-5927
(2003)
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PubMed id:
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Divergent evolutions of trinucleotide polymerization revealed by an archaeal CCA-adding enzyme structure.
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M.Okabe,
K.Tomita,
R.Ishitani,
R.Ishii,
N.Takeuchi,
F.Arisaka,
O.Nureki,
S.Yokoyama.
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ABSTRACT
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CCA-adding enzyme [ATP(CTP):tRNA nucleotidyltransferase], a template-independent
RNA polymerase, adds the defined 'cytidine-cytidine-adenosine' sequence onto the
3' end of tRNA. The archaeal CCA-adding enzyme (class I) and
eubacterial/eukaryotic CCA-adding enzyme (class II) show little amino acid
sequence homology, but catalyze the same reaction in a defined fashion. Here, we
present the crystal structures of the class I archaeal CCA-adding enzyme from
Archaeoglobus fulgidus, and its complexes with CTP and ATP at 2.0, 2.0 and 2.7 A
resolutions, respectively. The geometry of the catalytic carboxylates and the
relative positions of CTP and ATP to a single catalytic site are well conserved
in both classes of CCA-adding enzymes, whereas the overall architectures, except
for the catalytic core, of the class I and class II CCA-adding enzymes are
fundamentally different. Furthermore, the recognition mechanisms of substrate
nucleotides and tRNA molecules are distinct between these two classes,
suggesting that the catalytic domains of class I and class II enzymes share a
common origin, and distinct substrate recognition domains have been appended to
form the two presently divergent classes.
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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.Hoffmeier,
H.Betat,
A.Bluschke,
R.Günther,
S.Junghanns,
H.J.Hofmann,
and
M.Mörl
(2010).
Unusual evolution of a catalytic core element in CCA-adding enzymes.
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Nucleic Acids Res, 38,
4436-4447.
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B.Pan,
Y.Xiong,
and
T.A.Steitz
(2010).
How the CCA-adding enzyme selects adenine over cytosine at position 76 of tRNA.
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Science, 330,
937-940.
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PDB codes:
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Y.M.Hou
(2010).
CCA addition to tRNA: implications for tRNA quality control.
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IUBMB Life, 62,
251-260.
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M.Morar,
K.Bhullar,
D.W.Hughes,
M.Junop,
and
G.D.Wright
(2009).
Structure and mechanism of the lincosamide antibiotic adenylyltransferase LinB.
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Structure, 17,
1649-1659.
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PDB codes:
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Y.Toh,
D.Takeshita,
T.Numata,
S.Fukai,
O.Nureki,
and
K.Tomita
(2009).
Mechanism for the definition of elongation and termination by the class II CCA-adding enzyme.
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EMBO J, 28,
3353-3365.
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PDB codes:
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M.Dupasquier,
S.Kim,
K.Halkidis,
H.Gamper,
and
Y.M.Hou
(2008).
tRNA integrity is a prerequisite for rapid CCA addition: implication for quality control.
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J Mol Biol, 379,
579-588.
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X.Shan,
T.A.Russell,
S.M.Paul,
D.B.Kushner,
and
P.B.Joyce
(2008).
Characterization of a temperature-sensitive mutation that impairs the function of yeast tRNA nucleotidyltransferase.
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Yeast, 25,
219-233.
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Y.Toh,
T.Numata,
K.Watanabe,
D.Takeshita,
O.Nureki,
and
K.Tomita
(2008).
Molecular basis for maintenance of fidelity during the CCA-adding reaction by a CCA-adding enzyme.
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EMBO J, 27,
1944-1952.
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PDB codes:
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H.D.Cho,
C.L.Verlinde,
and
A.M.Weiner
(2007).
Reengineering CCA-adding enzymes to function as (U,G)- or dCdCdA-adding enzymes or poly(C,A) and poly(U,G) polymerases.
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Proc Natl Acad Sci U S A, 104,
54-59.
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H.D.Cho,
Y.Chen,
G.Varani,
and
A.M.Weiner
(2006).
A model for C74 addition by CCA-adding enzymes: C74 addition, like C75 and A76 addition, does not involve tRNA translocation.
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J Biol Chem, 281,
9801-9811.
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K.Tomita,
R.Ishitani,
S.Fukai,
and
O.Nureki
(2006).
Complete crystallographic analysis of the dynamics of CCA sequence addition.
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Nature, 443,
956-960.
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PDB codes:
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C.Lehmann,
S.Pullalarevu,
W.Krajewski,
M.A.Willis,
A.Galkin,
A.Howard,
and
O.Herzberg
(2005).
Structure of HI0073 from Haemophilus influenzae, the nucleotide-binding domain of a two-protein nucleotidyl transferase.
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Proteins, 60,
807-811.
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PDB code:
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H.D.Cho,
C.L.Verlinde,
and
A.M.Weiner
(2005).
Archaeal CCA-adding enzymes: central role of a highly conserved beta-turn motif in RNA polymerization without translocation.
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J Biol Chem, 280,
9555-9566.
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J.Deng,
N.L.Ernst,
S.Turley,
K.D.Stuart,
and
W.G.Hol
(2005).
Structural basis for UTP specificity of RNA editing TUTases from Trypanosoma brucei.
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EMBO J, 24,
4007-4017.
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PDB codes:
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A.M.Weiner
(2004).
tRNA maturation: RNA polymerization without a nucleic acid template.
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Curr Biol, 14,
R883-R885.
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G.Martin,
and
W.Keller
(2004).
Sequence motifs that distinguish ATP(CTP):tRNA nucleotidyl transferases from eubacterial poly(A) polymerases.
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RNA, 10,
899-906.
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H.D.Cho,
and
A.M.Weiner
(2004).
A single catalytically active subunit in the multimeric Sulfolobus shibatae CCA-adding enzyme can carry out all three steps of CCA addition.
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J Biol Chem, 279,
40130-40136.
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K.Tomita,
S.Fukai,
R.Ishitani,
T.Ueda,
N.Takeuchi,
D.G.Vassylyev,
and
O.Nureki
(2004).
Structural basis for template-independent RNA polymerization.
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Nature, 430,
700-704.
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PDB code:
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Y.Xiong,
and
T.A.Steitz
(2004).
Mechanism of transfer RNA maturation by CCA-adding enzyme without using an oligonucleotide template.
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Nature, 430,
640-645.
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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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