PDBsum entry: 1dp2

Transferase

PDB id: 1dp2

Contents

Protein chain

293 a.a. *

Ligands

LPB

Waters ×112

* Residue conservation analysis

PDB id:

1dp2

Name:

Transferase

Title:

Crystal structure of the complex between rhodanese and lipoa

Structure:

Rhodanese. Chain: a. Ec: 2.8.1.1

Source:

Bos taurus. Cattle. Organism_taxid: 9913

Resolution:

2.01Å R-factor: 0.170 R-free: 0.230

Authors:

G.Zanotti,M.Cianci

Key ref:

M.Cianci et al. (2000). Specific interaction of lipoate at the active site of rhodanese. Biochim Biophys Acta, 1481, 103-108. PubMed id: 11004580 DOI: 10.1016/S0167-4838(00)00114-X

Date:

23-Dec-99 Release date: 13-Dec-00

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: 10.1016/S0167-4838(00)00114-X

Biochim Biophys Acta 1481:103-108 (2000)

PubMed id: 11004580

Specific interaction of lipoate at the active site of rhodanese.

M.Cianci, F.Gliubich, G.Zanotti, R.Berni.

ABSTRACT

Dihydrolipoate is an acceptor of the rhodanese-bound sulfane sulfur atom, as shown by analysis of the elementary steps of the reaction catalyzed by rhodanese. The crystal structure of sulfur-substituted rhodanese complexed with the non-reactive oxidized form of lipoate has revealed that the compound is bound at the enzyme active site, with the dithiolane ring buried in the interior of the cavity and the carboxylic end pointing towards the solvent. One of the sulfur atoms of the ligand in the unproductive complex is relatively close to the sulfane sulfur bound to Cys-247, the sulfur that is transferred during the catalytic reaction. This mode of binding of lipoate is likely to mimic that of dihydrolipoate. The results presented here support the possible role of dihydrolipoate as sulfur-acceptor substrate of rhodanese in an enzymatic reaction that might serve to provide iron-sulfur proteins with inorganic sulfide.