spacer
spacer
Go to PDB code: 
protein links
Transferase(thiosulfate,cyanide sulfur) PDB id
1rhd
Jmol
Contents
Protein chain
293 a.a. *
* Residue conservation analysis
PDB id:
1rhd
Name: Transferase(thiosulfate,cyanide sulfur)
Title: Structure of bovine liver rhodanese. I. Structure determination at 2.5 angstroms resolution and a comparison of the conformation and sequence of its two domains
Structure: Rhodanese. Chain: a. Engineered: yes
Source: Bos taurus. Cattle. Organism_taxid: 9913
Resolution:
2.50Å     R-factor:   not given    
Authors: W.G.J.Hol,J.H.Ploegman,K.H.Kalk,G.Drent
Key ref:
J.H.Ploegman et al. (1978). Structure of bovine liver rhodanese. I. Structure determination at 2.5 A resolution and a comparison of the conformation and sequence of its two domains. J Mol Biol, 123, 557-594. PubMed id: 691057 DOI: 10.1016/0022-2836(78)90207-3
Date:
23-Nov-77     Release date:   16-Jan-78    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P00586  (THTR_BOVIN) -  Thiosulfate sulfurtransferase
Seq:
Struc: 		297 a.a.
293 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 3 residue positions (black crosses)

 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     plasma membrane   4 terms 
  Biological process     rRNA transport   1 term 
  Biochemical function     transferase activity     4 terms  

 

 
    reference    
 
 
DOI no: 10.1016/0022-2836(78)90207-3 J Mol Biol 123:557-594 (1978)
PubMed id: 691057  
 
 
Structure of bovine liver rhodanese. I. Structure determination at 2.5 A resolution and a comparison of the conformation and sequence of its two domains.
J.H.Ploegman, G.Drent, K.H.Kalk, W.G.Hol.
 
  ABSTRACT  
 
No abstract given.

 
  Selected figure(s)  
 
Figure 11.
FIG. 11. Stereopictur f the esidues of he hydrophobic luster ' in omain II superimposed on thse of he ydrophobic cluster B in omain . he residues in omain are indicated with double bonds, hose in domain II with ingle bonds. Rotation nd translation parameters are given n Table 11. 		Figure 15.
FIG. 15. ydrogen-bonding schemes of the pleated-seet regions of LADHase a), rhodanese b) en lavodoxin c), The arros indicate H + CO. he broken &mows indicate possible hydrogen bonds. The residues used or comparison are within the outlined area. Residue 27 in hodmese has no counterpart in lavodoxin and is herefore not used in the comparison ith this protein.
 
  The above figures are reprinted by permission from Elsevier: J Mol Biol (1978, 123, 557-594) copyright 1978.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
19536635 O.T.Akinsiku, F.K.Agboola, A.Kuku, and A.Afolayan (2010).
Physicochemical and kinetic characteristics of rhodanese from the liver of African catfish Clarias gariepinus Burchell in Asejire lake.
  Fish Physiol Biochem, 36, 573-586.  
17442671 J.Andrade, A.Karmali, M.A.Carrondo, and C.Frazão (2007).
Structure of amidase from Pseudomonas aeruginosa showing a trapped acyl transfer reaction intermediate state.
  J Biol Chem, 282, 19598-19605.
PDB code: 2uxy
17400920 X.Tao, and L.Tong (2007).
Crystal structure of the MAP kinase binding domain and the catalytic domain of human MKP5.
  Protein Sci, 16, 880-886.
PDB codes: 2ouc 2oud
17360617 Y.Kipnis, N.Papo, G.Haran, and A.Horovitz (2007).
Concerted ATP-induced allosteric transitions in GroEL facilitate release of protein substrate domains in an all-or-none manner.
  Proc Natl Acad Sci U S A, 104, 3119-3124.  
16680676 M.Hattori, E.Mizohata, A.Tatsuguchi, R.Shibata, S.Kishishita, K.Murayama, T.Terada, S.Kuramitsu, M.Shirouzu, and S.Yokoyama (2006).
Crystal structure of the single-domain rhodanese homologue TTHA0613 from Thermus thermophilus HB8.
  Proteins, 64, 284-287.
PDB code: 1wv9
17136732 Z.Prokop, F.Oplustil, J.DeFrank, and J.Damborský (2006).
Enzymes fight chemical weapons.
  Biotechnol J, 1, 1370-1380.  
15576557 D.Pantoja-Uceda, B.López-Méndez, S.Koshiba, M.Inoue, T.Kigawa, T.Terada, M.Shirouzu, A.Tanaka, M.Seki, K.Shinozaki, S.Yokoyama, and P.Güntert (2005).
Solution structure of the rhodanese homology domain At4g01050(175-295) from Arabidopsis thaliana.
  Protein Sci, 14, 224-230.
PDB code: 1vee
15805776 M.Acosta, S.Beard, J.Ponce, M.Vera, J.C.Mobarec, and C.A.Jerez (2005).
Identification of putative sulfurtransferase genes in the extremophilic Acidithiobacillus ferrooxidans ATCC 23270 genome: structural and functional characterization of the proteins.
  OMICS, 9, 13-29.  
12952945 M.S.Alphey, R.A.Williams, J.C.Mottram, G.H.Coombs, and W.N.Hunter (2003).
The crystal structure of Leishmania major 3-mercaptopyruvate sulfurtransferase. A three-domain architecture with a serine protease-like triad at the active site.
  J Biol Chem, 278, 48219-48227.
PDB code: 1okg
12513527 A.M.Walczak, and J.M.Antosiewicz (2002).
Langevin dynamics of proteins at constant pH.
  Phys Rev E Stat Nonlin Soft Matter Phys, 66, 051911.  
10809729 A.M.Bhattacharyya, and P.Horowitz (2000).
Alteration around the active site of rhodanese during urea-induced denaturation and its implications for folding.
  J Biol Chem, 275, 14860-14864.  
11106482 S.J.Cooper, C.D.Garner, W.R.Hagen, P.F.Lindley, and S.Bailey (2000).
Hybrid-cluster protein (HCP) from Desulfovibrio vulgaris (Hildenborough) at 1.6 A resolution.
  Biochemistry, 39, 15044-15054.
PDB codes: 1e1d 1e2u
11112515 T.Wieprecht, O.Apostolov, M.Beyermann, and J.Seelig (2000).
Interaction of a mitochondrial presequence with lipid membranes: role of helix formation for membrane binding and perturbation.
  Biochemistry, 39, 15297-15305.  
  10211836 D.R.Westhead, T.W.Slidel, T.P.Flores, and J.M.Thornton (1999).
Protein structural topology: Automated analysis and diagrammatic representation.
  Protein Sci, 8, 897-904.  
10559274 T.Shibatani, G.Kramer, B.Hardesty, and P.M.Horowitz (1999).
Domain separation precedes global unfolding of rhodanese.
  J Biol Chem, 274, 33795-33799.  
9188741 A.V.Efimov (1997).
Structural trees for protein superfamilies.
  Proteins, 28, 241-260.  
9071024 T.Shirai, and M.Go (1997).
Adaptive amino acid replacements accompanied by domain fusion in reverse transcriptase.
  J Mol Evol, 44, S155-S162.  
8628732 A.Amadei, and B.Vallone (1996).
Identification of a pattern in protein structure based on energetic and statistical considerations.
  Proteins, 24, 35-50.  
8910318 N.Nagahara, and T.Nishino (1996).
Role of amino acid residues in the active site of rat liver mercaptopyruvate sulfurtransferase. CDNA cloning, overexpression, and site-directed mutagenesis.
  J Biol Chem, 271, 27395-27401.  
8617271 R.Colnaghi, S.Pagani, C.Kennedy, and M.Drummond (1996).
Cloning, sequence analysis and overexpression of the rhodanese gene of Azotobacter vinelandii.
  Eur J Biochem, 236, 240-248.  
  7773168 M.B.Swindells (1995).
A procedure for detecting structural domains in proteins.
  Protein Sci, 4, 103-112.  
7608189 N.Nagahara, T.Okazaki, and T.Nishino (1995).
Cytosolic mercaptopyruvate sulfurtransferase is evolutionarily related to mitochondrial rhodanese. Striking similarity in active site amino acid sequence and the increase in the mercaptopyruvate sulfurtransferase activity of rhodanese by site-directed mutagenesis.
  J Biol Chem, 270, 16230-16235.  
8130328 G.M.Lipkind, and H.A.Fozzard (1994).
A structural model of the tetrodotoxin and saxitoxin binding site of the Na+ channel.
  Biophys J, 66, 1.  
  7516875 P.Dumas, M.Bergdoll, C.Cagnon, and J.M.Masson (1994).
Crystal structure and site-directed mutagenesis of a bleomycin resistance protein and their significance for drug sequestering.
  EMBO J, 13, 2483-2492.
PDB code: 1byl
8456096 M.K.Gilson (1993).
Multiple-site titration and molecular modeling: two rapid methods for computing energies and forces for ionizable groups in proteins.
  Proteins, 15, 266-282.  
8451241 N.Vtyurin (1993).
The role of local tight packing of hydrophobic groups in beta-structure.
  Proteins, 15, 62-70.  
2017436 C.Sander, and R.Schneider (1991).
Database of homology-derived protein structures and the structural meaning of sequence alignment.
  Proteins, 9, 56-68.  
  1708376 D.E.Laudenbach, D.Ehrhardt, L.Green, and A.Grossman (1991).
Isolation and characterization of a sulfur-regulated gene encoding a periplasmically localized protein with sequence similarity to rhodanese.
  J Bacteriol, 173, 2751-2760.  
1660134 G.Vriend, and C.Sander (1991).
Detection of common three-dimensional substructures in proteins.
  Proteins, 11, 52-58.  
1961713 R.Nussinov, and H.J.Wolfson (1991).
Efficient detection of three-dimensional structural motifs in biological macromolecules by computer vision techniques.
  Proc Natl Acad Sci U S A, 88, 10495-10499.  
1708883 P.A.Rice, A.Goldman, and T.A.Steitz (1990).
A helix-turn-strand structural motif common in alpha-beta proteins.
  Proteins, 8, 334-340.  
2275748 R.A.Kohanski, and R.L.Heinrikson (1990).
Primary structure of avian hepatic rhodanese.
  J Protein Chem, 9, 369-377.  
2096889 W.C.Thresher, and H.E.Swaisgood (1990).
Characterization of specific interactions of coenzymes, regulatory nucleotides and cibacron blue with nucleotide binding domains of enzymes by analytical affinity chromatography.
  J Mol Recognit, 3, 220-228.  
3287370 M.K.Gilson, and B.H.Honig (1988).
Energetics of charge-charge interactions in proteins.
  Proteins, 3, 32-52.  
3186692 M.K.Gilson, and B.Honig (1988).
Calculation of the total electrostatic energy of a macromolecular system: solvation energies, binding energies, and conformational analysis.
  Proteins, 4, 7.  
3191921 P.J.Kooystra, K.H.Kalk, and W.G.Hol (1988).
Soaking in Cs2SO4 reveals a caesium-aromatic interaction in bovine-liver rhodanese.
  Eur J Biochem, 177, 345-349.  
  3019675 E.Littler, J.Zeuthen, A.A.McBride, E.Trøst Sørensen, K.L.Powell, J.E.Walsh-Arrand, and J.R.Arrand (1986).
Identification of an Epstein-Barr virus-coded thymidine kinase.
  EMBO J, 5, 1959-1966.  
2983992 F.Bonomi, S.Pagani, and D.M.Kurtz (1985).
Enzymic synthesis of the 4Fe-4S clusters of Clostridium pasteurianum ferredoxin.
  Eur J Biochem, 148, 67-73.  
2410917 I.A.Wilson, D.H.Haft, E.D.Getzoff, J.A.Tainer, R.A.Lerner, and S.Brenner (1985).
Identical short peptide sequences in unrelated proteins can have different conformations: a testing ground for theories of immune recognition.
  Proc Natl Acad Sci U S A, 82, 5255-5259.  
6442358 A.A.Zharkikh, V.V.Solovyov, and N.A.Kolchanov (1984).
Conformational changes in the globin family during evolution. 1. Analysis of the evolutionary role of insertions and deletions.
  J Mol Evol, 21, 42-53.  
6442995 L.H.Weaver, M.G.Grütter, S.J.Remington, T.M.Gray, N.W.Isaacs, and B.W.Matthews (1984).
Comparison of goose-type, chicken-type, and phage-type lysozymes illustrates the changes that occur in both amino acid sequence and three-dimensional structure during evolution.
  J Mol Evol, 21, 97.  
6589161 L.J.Lijk, C.A.Torfs, K.H.Kalk, M.C.De Maeyer, and W.G.Hol (1984).
Differences in the binding of sulfate, selenate and thiosulfate ions to bovine liver rhodanese, and a description of a binding site for ammonium and sodium ions. An X-ray diffraction study.
  Eur J Biochem, 142, 399-408.  
6304705 M.R.Pincus, F.Gerewitz, R.H.Schwartz, and H.A.Scheraga (1983).
Correlation between the conformation of cytochrome c peptides and their stimulatory activity in a T-lymphocyte proliferation assay.
  Proc Natl Acad Sci U S A, 80, 3297-3300.  
6832137 P.Argos, and R.J.Siezen (1983).
Structural homology of lens crystallins. A method to detect protein structural homology from primary sequences.
  Eur J Biochem, 131, 143-148.  
6946927 C.Cannella, M.Costa, B.Pensa, G.Ricci, L.Pecci, and D.Cavallini (1981).
Multiple forms of bovine liver rhodanese.
  Eur J Biochem, 119, 491-495.  
7411653 A.D.McLachlan (1980).
Repeated structure and possible gene duplications in high potential iron protein and rubredoxin.
  J Mol Evol, 15, 309-315.  
385312 A.D.McLachlan (1979).
Gene duplication in the evolution of the yeast hexokinase active site.
  Eur J Biochem, 100, 181-187.  
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 code is shown on the right.