spacer
spacer
Go to PDB code: 
protein links
Structural genomics, unknown function PDB id
1tq1
Jmol
Contents
Protein chain
119 a.a. *
* Residue conservation analysis
PDB id:
1tq1
Name: Structural genomics, unknown function
Title: Solution structure of at5g66040, a putative protein from arabidosis thaliana
Structure: Senescence-associated family protein. Chain: a. Synonym: at5g66040. Engineered: yes
Source: Arabidopsis thaliana. Thale cress. Organism_taxid: 3702. Expressed in: cell-free synthesis. Other_details: wheat germ cell-free, in vitro expression
NMR struc: 5 models
Authors: C.C.Cornilescu,G.Cornilescu,S.Singh,M.S.Lee,E.M.Tyler, M.N.Shahan,D.Vinarov,J.L.Markley,Center For Eukaryotic Structural Genomics (Cesg)
Key ref:
G.Cornilescu et al. (2006). Solution structure of a single-domain thiosulfate sulfurtransferase from Arabidopsis thaliana. Protein Sci, 15, 2836-2841. PubMed id: 17088324 DOI: 10.1110/ps.062395206
Date:
16-Jun-04     Release date:   29-Jun-04    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q39129  (STR16_ARATH) -  Thiosulfate sulfurtransferase, chloroplastic
Seq:
Struc:
120 a.a.
119 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.2.8.1.1  - Thiosulfate sulfurtransferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Thiosulfate + cyanide = sulfite + thiocyanate
Thiosulfate
+ cyanide
= sulfite
+ thiocyanate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     plastid   2 terms 
  Biochemical function     transferase activity     2 terms  

 

 
    reference    
 
 
DOI no: 10.1110/ps.062395206 Protein Sci 15:2836-2841 (2006)
PubMed id: 17088324  
 
 
Solution structure of a single-domain thiosulfate sulfurtransferase from Arabidopsis thaliana.
G.Cornilescu, D.A.Vinarov, E.M.Tyler, J.L.Markley, C.C.Cornilescu.
 
  ABSTRACT  
 
We describe the three-dimensional structure of the product of Arabidopsis thaliana gene At5g66040.1 as determined by NMR spectroscopy. This protein is categorized as single-domain sulfurtransferase and is annotated as a senescence-associated protein (sen1-like protein) and ketoconazole resistance protein (http://arabidopsis.org/info/genefamily/STR_genefamily.html). The sequence of At5g66040.1 is virtually identical to that of a protein from Arabidopsis found by others to confer ketoconazole resistance in yeast. Comparison of the three-dimensional structure with those in the Protein Data Bank revealed that At5g66040.1 contains an additional mobile beta-hairpin not found in other rhodaneses that may function in binding specific substrates. This represents the first structure of a single-domain plant sulfurtransferase. The enzymatically active cysteine-containing domain belongs to the CDC25 class of phosphatases, sulfide dehydrogenases, and stress proteins such as senescence specific protein 1 in plants, PspE and GlpE in bacteria, and cyanide and arsenate resistance proteins. Versions of this domain that lack the active site cysteine are found in other proteins, such as phosphatases, ubiquitin hydrolases, and sulfuryltransferases.
 
  Selected figure(s)  
 
Figure 3.
Figure 3. (A) Comparison of ribbon diagrams for At5g66040.1; GlpE, an Str from E. coli (PDB ID 1GMX); a polysulfide-sulfur
 
  The above figure is reprinted by permission from the Protein Society: Protein Sci (2006, 15, 2836-2841) copyright 2006.  
  Figure was selected by the author.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
20135153 J.Papenbrock, S.Guretzki, and M.Henne (2011).
Latest news about the sulfurtransferase protein family of higher plants.
  Amino Acids, 41, 43-57.  
17697123 M.C.Giuliani, P.Tron, G.Leroy, C.Aubert, P.Tauc, and M.T.Giudici-Orticoni (2007).
A new sulfurtransferase from the hyperthermophilic bacterium Aquifex aeolicus. Being single is not so simple when temperature gets high.
  FEBS J, 274, 4572-4587.  
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.