 |
PDBsum entry 2fyh
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
|
PDB id:
|
|
|
|
| Name: |
|
Ligase
|
|
|
Title:
|
|
Solution structure of the 2'-5' RNA ligase-like protein from pyrococcus furiosus
|
|
Structure:
|
|
Putative integral membrane transport protein. Chain: a. Synonym: 2'-5' RNA ligase-like protein. Engineered: yes
|
|
Source:
|
|
Pyrococcus furiosus. Organism_taxid: 186497. Strain: dsm3638. Gene: pf0027. Expressed in: escherichia coli. Expression_system_taxid: 469008.
|
|
NMR struc:
|
|
20 models
|
|
|
Authors:
|
|
K.Okada,T.Matsuda,T.Sakamoto,Y.Muto,S.Yokoyama,A.Kanai,G.Kawai,Riken Structural Genomics/proteomics Initiative (Rsgi)
|
|
Key ref:
|
|
A.Kanai
et al.
(2009).
Characterization of a heat-stable enzyme possessing GTP-dependent RNA ligase activity from a hyperthermophilic archaeon, Pyrococcus furiosus.
Rna,
15,
420-431.
PubMed id:
|
|
|
Date:
|
|
|
08-Feb-06
|
Release date:
|
20-Feb-07
|
|
|
|
|
|
|
PROCHECK
|
|
|
|
|
|
Headers
|
|
|
|
References
|
|
|
|
|
|
|
|
Q8U4Q3
(THPR_PYRFU) -
RNA 2',3'-cyclic phosphodiesterase from Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
|
|
|
|
Seq:
Struc:
|
|
|
|
184 a.a.
190 a.a.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Key: |
 |
PfamA domain |
|
|
 |
Secondary structure |
|
 |
CATH domain |
|
|
|
|
|
|
|
|
|
|
|
|
|
Enzyme class:
|
|
E.C.3.1.4.58
- Rna 2',3'-cyclic 3'-phosphodiesterase.
|
|
|
|
|
|
|
Reaction:
|
|
a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + H2O = a 3'-end 2'-phospho-ribonucleotide-RNA + H+
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
| |
|
|
Rna
15:420-431
(2009)
|
|
PubMed id:
|
|
|
|
|
|
| |
|
Characterization of a heat-stable enzyme possessing GTP-dependent RNA ligase activity from a hyperthermophilic archaeon, Pyrococcus furiosus.
|
|
A.Kanai,
A.Sato,
Y.Fukuda,
K.Okada,
T.Matsuda,
T.Sakamoto,
Y.Muto,
S.Yokoyama,
G.Kawai,
M.Tomita.
|
|
|
|
|
| |
ABSTRACT
|
|
|
|
| |
|
|
Using an expression protein library of a hyperthermophilic archaeon, Pyrococcus
furiosus, we identified a gene (PF0027) that encodes a protein with heat-stable
cyclic nucleotide phosphodiesterase (CPDase) activity. The PF0027 gene encoded a
21-kDa protein and an amino acid sequence that showed approximately 27% identity
to that of the 2'-5' tRNA ligase protein, ligT (20 kDa), from Escherichia coli.
We found that the purified PF0027 protein possessed GTP-dependent RNA ligase
activity and that synthetic tRNA halves bearing 2',3'-cyclic phosphate and 5'-OH
termini were substrates for the ligation reaction in vitro. GTP hydrolysis was
not required for the reaction, and GTPgammaS enhanced the tRNA ligation activity
of PF0027 protein, suggesting that the ligation step is regulated by a novel
mechanism. In comparison to the strong CPDase activity of the PF0027 protein,
the RNA ligase activity itself was quite weak, and the ligation product was
unstable during in vitro reaction. Finally, we used NMR to determine the
solution structure of the PF0027 protein and discuss the implications of our
results in understanding the role of the PF0027 protein.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
 |
 |
|
Literature references that cite this PDB file's key reference
|
|
|
| |
PubMed id
|
|
Reference
|
|
|
|
|
|
M.Englert,
K.Sheppard,
A.Aslanian,
J.R.Yates,
and
D.Söll
(2011).
Archaeal 3'-phosphate RNA splicing ligase characterization identifies the missing component in tRNA maturation.
|
| |
Proc Natl Acad Sci U S A,
108,
1290-1295.
|
|
|
|
|
|
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.
|
|
Links
