PDBsum entry: 1rhs

Transferase

PDB id: 1rhs

Contents

Protein chain

293 a.a. *

Waters ×407

* Residue conservation analysis

PDB id:

1rhs

Name:

Transferase

Title:

Sulfur-substituted rhodanese

Structure:

Sulfur-substituted rhodanese. Chain: a. Ec: 2.8.1.1

Source:

Bos taurus. Cattle. Organism_taxid: 9913. Organ: liver. Cellular_location: cytoplasm

Resolution:

1.36Å R-factor: 0.169 R-free: 0.229

Authors:

G.Zanotti,F.Gliubich,M.Colapietro,L.Barba

Key ref:

F.Gliubich et al. (1996). Active site structural features for chemically modified forms of rhodanese. J Biol Chem, 271, 21054-21061. PubMed id: 8702871 DOI: 10.1074/jbc.271.35.21054

Date:

16-Jul-97 Release date: 21-Jan-98

Protein chain

P00586  (THTR_BOVIN) -  Thiosulfate sulfurtransferase

Seq: 297 a.a.

Struc: 293 a.a.

Enzyme reactions

• Enzyme class: E.C.2.8.1.1 - Thiosulfate sulfurtransferase.
• Reaction: Thiosulfate + cyanide = sulfite + thiocyanate

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 Gene Ontology (GO) functional annotation 

• Cellular component: plasma membrane (4 terms)
• Biological process: rRNA transport (1 term)
• Biochemical function: transferase activity (4 terms)

reference

DOI no: 10.1074/jbc.271.35.21054

J Biol Chem 271:21054-21061 (1996)

PubMed id: 8702871

Active site structural features for chemically modified forms of rhodanese.

F.Gliubich, M.Gazerro, G.Zanotti, S.Delbono, G.Bombieri, R.Berni.

ABSTRACT

In the course of the reaction catalyzed by rhodanese, the enzyme cycles between two catalytic intermediates, the sulfur-free and the sulfur-substituted (persulfide-containing) forms. The crystal structure of sulfur-free rhodanese, which was prepared in solution and then crystallized, is highly similar to that of sulfur-substituted enzyme. The inactivation of sulfur-free rhodanese with a small molar excess of hydrogen peroxide relies essentially on a modification limited to the active site, consisting of the oxidation of the essential sulfhydryl to sulfenyl group (-S-OH). Upon reaction of the sulfur-free enzyme with monoiodoacetate in the crystal, the Cys-247 side chain with the bound carboxymethyl group is forced into a conformation that allows favorable interactions of the carboxylate with the four peptide NH groups that participate in hydrogen bonding interactions with the transferable sulfur atom of the persulfide group in the sulfur-substituted rhodanese. It is concluded that active site-specific chemical modifications of sulfur-free rhodanese do not lead to significant changes of the protein structure, consistent with a high degree of similarity of the structures of the sulfur-free and sulfur-substituted forms of the enzyme both in solution and in the crystal.

Selected figure(s)

Figure 2.
Fig. 2. R.m.s. deviation between equivalent C atoms of our model of sulfur containing rhodanese and that of Ploegman et al. (1979).

Figure 4.
Fig. 4. Stereo view of a portion of the active site of rhodanese for: A, sulfur-containing form of the enzyme; B, sulfur-free form. Dashed lines indicate hydrogen bonding interactions between S or S of Cys-247 and NH groups of the backbone.

The above figures are reprinted by permission from the ASBMB: J Biol Chem (1996, 271, 21054-21061) copyright 1996.

Figures were selected by an automated process.