 |
PDBsum entry 1k4h
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
|
PDB id:
|
|
|
|
| Name: |
|
Transferase
|
|
|
Title:
|
|
Crystal structure of tRNA-guanine transglycosylase (tgt) complexed with 2,6-diamino-8-propylsulfanylmethyl-3h-quinazoline-4-one
|
|
Structure:
|
|
tRNA-guanine-transglycosylase. Chain: a. Synonym: tgt, queuine tRNA-ribosyltransferase, guanine insertion enzyme. Engineered: yes
|
|
Source:
|
|
Zymomonas mobilis. Organism_taxid: 542. Expressed in: escherichia coli. Expression_system_taxid: 562
|
|
Biol. unit:
|
|
Dimer (from
)
|
|
Resolution:
|
|
|
1.80Å
|
R-factor:
|
0.196
|
R-free:
|
0.229
|
|
|
Authors:
|
|
R.Brenk,E.A.Meyer,R.K.Castellano,M.Furler,M.T.Stubbs,G.Klebe, F.Diederich
|
|
Key ref:
|
|
E.A.Meyer
et al.
(2002).
De novo design, synthesis, and in vitro evaluation of inhibitors for prokaryotic tRNA-guanine transglycosylase: a dramatic sulfur effect on binding affinity.
Chembiochem,
3,
250-253.
PubMed id:
DOI:
|
|
|
Date:
|
|
|
08-Oct-01
|
Release date:
|
24-Apr-02
|
|
|
|
|
|
|
PROCHECK
|
|
|
|
|
|
Headers
|
|
|
|
References
|
|
|
|
|
|
|
|
P28720
(TGT_ZYMMO) -
Queuine tRNA-ribosyltransferase from Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
|
|
|
|
Seq:
Struc:
|
|
|
|
386 a.a.
372 a.a.*
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Key: |
 |
PfamA domain |
|
|
 |
Secondary structure |
|
 |
CATH domain |
|
|
*
PDB and UniProt seqs differ
at 1 residue position (black
cross)
|
|
|
|
|
|
|
|
|
|
|
|
|
Enzyme class:
|
|
E.C.2.4.2.29
- tRNA-guanosine(34) preQ1 transglycosylase.
|
|
|
|
|
|
|
Reaction:
|
|
7-aminomethyl-7-carbaguanine + guanosine34 in tRNA = 7-aminomethyl-7- carbaguanosine34 in tRNA + guanine
|
|
|
|
|
|
7-aminomethyl-7-carbaguanine
Bound ligand (Het Group name = )
matches with 55.00% similarity
|
+
|
guanosine(34) in tRNA
|
=
|
7-aminomethyl-7- carbaguanosine(34) in tRNA
|
+
|
guanine
|
|
|
|
|
|
|
|
|
|
|
|
|
Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
| |
|
|
| |
|
DOI no:
|
Chembiochem
3:250-253
(2002)
|
|
PubMed id:
|
|
|
|
|
|
| |
|
De novo design, synthesis, and in vitro evaluation of inhibitors for prokaryotic tRNA-guanine transglycosylase: a dramatic sulfur effect on binding affinity.
|
|
E.A.Meyer,
R.Brenk,
R.K.Castellano,
M.Furler,
G.Klebe,
F.Diederich.
|
|
|
|
|
| |
ABSTRACT
|
|
|
|
| |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
 |
 |
|
Literature references that cite this PDB file's key reference
|
|
|
| |
PubMed id
|
|
Reference
|
|
|
|
|
|
A.Goel,
F.V.Singh,
M.Dixit,
D.Verma,
R.Raghunandan,
and
P.R.Maulik
(2007).
Highly efficient non-palladium-catalyzed controlled synthesis and X-ray analysis of functionalized 1,2-diaryl-, 1,2,3-triaryl-, and 1,2,3,4-tetraarylbenzenes.
|
| |
Chem Asian J,
2,
239-247.
|
|
|
|
|
|
|
B.Stengl,
K.Reuter,
and
G.Klebe
(2005).
Mechanism and substrate specificity of tRNA-guanine transglycosylases (TGTs): tRNA-modifying enzymes from the three different kingdoms of life share a common catalytic mechanism.
|
| |
Chembiochem,
6,
1926-1939.
|
|
|
|
|
|
|
O.Kraemer,
I.Hazemann,
A.D.Podjarny,
and
G.Klebe
(2004).
Virtual screening for inhibitors of human aldose reductase.
|
| |
Proteins,
55,
814-823.
|
|
|
|
|
|
|
S.C.Miller,
and
T.J.Mitchison
(2004).
Synthesis and phenotypic screening of a Guanine-mimetic library.
|
| |
Chembiochem,
5,
1010-1012.
|
|
|
|
|
|
|
S.Sahli,
B.Stump,
T.Welti,
D.Blum-Kaelin,
J.D.Aebi,
C.Oefner,
H.J.Böhm,
and
F.Diederich
(2004).
Structure-based design, synthesis, and in vitro evaluation of nonpeptidic neprilysin inhibitors.
|
| |
Chembiochem,
5,
996.
|
|
|
|
|
|
|
R.Brenk,
M.T.Stubbs,
A.Heine,
K.Reuter,
and
G.Klebe
(2003).
Flexible adaptations in the structure of the tRNA-modifying enzyme tRNA-guanine transglycosylase and their implications for substrate selectivity, reaction mechanism and structure-based drug design.
|
| |
Chembiochem,
4,
1066-1077.
|
|
|
PDB codes:
|
|
|
|
|
|
|
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.
|
|
Links
