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PDBsum entry 3ipo

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protein ligands metals Protein-protein interface(s) links
Transferase PDB id
3ipo
Jmol
Contents
Protein chains
412 a.a. *
Ligands
PO4 ×2
PE4
GOL
PG0 ×2
Metals
_NA ×2
Waters ×560
* Residue conservation analysis
PDB id:
3ipo
Name: Transferase
Title: Crystal structure of ynje
Structure: Putative thiosulfate sulfurtransferase ynje. Chain: a, b. Engineered: yes
Source: Escherichia coli k-12. Organism_taxid: 83333. Strain: escherichia coli. Gene: b1757, jw5287, ynje. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.
Resolution:
2.40Å     R-factor:   0.161     R-free:   0.211
Authors: P.Haenzelmann,J.Kuper,H.Schindelin
Key ref: P.Hänzelmann et al. (2009). Crystal structure of YnjE from Escherichia coli, a sulfurtransferase with three rhodanese domains. Protein Sci, 18, 2480-2491. PubMed id: 19798741
Date:
18-Aug-09     Release date:   08-Dec-09    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P78067  (YNJE_ECOLI) -  Thiosulfate sulfurtransferase YnjE
Seq:
Struc:
435 a.a.
412 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 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!
  Biochemical function     thiosulfate sulfurtransferase activity     1 term  

 

 
    reference    
 
 
Protein Sci 18:2480-2491 (2009)
PubMed id: 19798741  
 
 
Crystal structure of YnjE from Escherichia coli, a sulfurtransferase with three rhodanese domains.
P.Hänzelmann, J.U.Dahl, J.Kuper, A.Urban, U.Müller-Theissen, S.Leimkühler, H.Schindelin.
 
  ABSTRACT  
 
Rhodaneses/sulfurtransferases are ubiquitous enzymes that catalyze the transfer of sulfane sulfur from a donor molecule to a thiophilic acceptor via an active site cysteine that is modified to a persulfide during the reaction. Here, we present the first crystal structure of a triple-domain rhodanese-like protein, namely YnjE from Escherichia coli, in two states where its active site cysteine is either unmodified or present as a persulfide. Compared to well-characterized tandem domain rhodaneses, which are composed of one inactive and one active domain, YnjE contains an extra N-terminal inactive rhodanese-like domain. Phylogenetic analysis reveals that YnjE triple-domain homologs can be found in a variety of other gamma-proteobacteria, in addition, some single-, tandem-, four and even six-domain variants exist. All YnjE rhodaneses are characterized by a highly conserved active site loop (CGTGWR) and evolved independently from other rhodaneses, thus forming their own subfamily. On the basis of structural comparisons with other rhodaneses and kinetic studies, YnjE, which is more similar to thiosulfate:cyanide sulfurtransferases than to 3-mercaptopyruvate:cyanide sulfurtransferases, has a different substrate specificity that depends not only on the composition of the active site loop with the catalytic cysteine at the first position but also on the surrounding residues. In vitro YnjE can be efficiently persulfurated by the cysteine desulfurase IscS. The catalytic site is located within an elongated cleft, formed by the central and C-terminal domain and is lined by bulky hydrophobic residues with the catalytic active cysteine largely shielded from the solvent.