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PDBsum entry 1k4g

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protein ligands metals links
Transferase PDB id
1k4g
Jmol
Contents
Protein chain
372 a.a. *
Ligands
AIQ
Metals
_ZN
Waters ×382
* Residue conservation analysis
PDB id:
1k4g
Name: Transferase
Title: Crystal structure of tRNA-guanine transglycosylase (tgt) com with 2,6-diamino-8-(1h-imidazol-2-ylsulfanylmethyl)-3h-quin one
Structure: tRNA-guanine transglycosylase. Chain: a. Synonym: tgt, queuine tRNA-ribosyltransferase, guanine inse enzyme. Engineered: yes
Source: Zymomonas mobilis. Organism_taxid: 542. Expressed in: escherichia coli. Expression_system_taxid: 562
Biol. unit: Dimer (from PQS)
Resolution:
1.70Å     R-factor:   0.199     R-free:   0.241
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: 11921407 DOI: 10.1002/1439-7633(20020301)3:2/3<250::AID-CBIC250>3.0.CO;2-J
Date:
08-Oct-01     Release date:   24-Apr-02    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P28720  (TGT_ZYMMO) -  Queuine tRNA-ribosyltransferase
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 reactions 
   Enzyme class: E.C.2.4.2.29  - tRNA-guanine(34) transglycosylase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction:
1. Guanine34 in tRNA + queuine = queuosine34 in tRNA + guanine
2. Guanine34 in tRNA + 7-aminomethyl-7-carbaguanine = 7-aminomethyl-7- carbaguanine34 in tRNA + guanine
Guanine(34) in tRNA
+
queuine
Bound ligand (Het Group name = AIQ)
matches with 50.00% similarity
= queuosine(34) in tRNA
+ guanine
Guanine(34) in tRNA
+
7-aminomethyl-7-carbaguanine
Bound ligand (Het Group name = AIQ)
matches with 50.00% similarity
= 7-aminomethyl-7- carbaguanine(34) in tRNA
+ guanine
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     tRNA processing   3 terms 
  Biochemical function     transferase activity     4 terms  

 

 
    reference    
 
 
DOI no: 10.1002/1439-7633(20020301)3:2/3<250::AID-CBIC250>3.0.CO;2-J Chembiochem 3:250-253 (2002)
PubMed id: 11921407  
 
 
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  
 
No abstract given.

 

Literature references that cite this PDB file's key reference

  PubMed id Reference
17441158 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.  
16206323 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.  
15146480 O.Kraemer, I.Hazemann, A.D.Podjarny, and G.Klebe (2004).
Virtual screening for inhibitors of human aldose reductase.
  Proteins, 55, 814-823.  
15239063 S.C.Miller, and T.J.Mitchison (2004).
Synthesis and phenotypic screening of a Guanine-mimetic library.
  Chembiochem, 5, 1010-1012.  
15239059 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.  
14523925 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: 1ozm 1ozq 1p0b 1p0d 1p0e
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