PDBsum entry 4u3e

Oxidoreductase

PDB id: 4u3e

Contents

Protein chains

637 a.a.

Ligands

CIT ×2

GOL ×2

ACT

Metals

_ZN ×2

_NA

Waters ×894

PDB id:

4u3e

Name:

Oxidoreductase

Title:

Anaerobic ribonucleotide reductase

Structure:

Ribonucleoside triphosphate reductase. Chain: a, b. Synonym: ribonucleotide reductase of class iii (anaerobic), large subunit, uncharacterized protein. Engineered: yes

Source:

Thermotoga maritima. Organism_taxid: 2336. Gene: tm_0385, thema_02795, tmari_0383. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

1.64Å R-factor: 0.171 R-free: 0.200

Authors:

M.A.Funk,C.L.Drennan

Key ref:

Y.Wei et al. (2014). The class III ribonucleotide reductase from Neisseria bacilliformis can utilize thioredoxin as a reductant. Proc Natl Acad Sci U S A, 111, E3756. PubMed id: 25157154 DOI: 10.1073/pnas.1414396111

Date:

20-Jul-14 Release date: 03-Sep-14

Protein chains

Q9WYL6  (Q9WYL6_THEMA) -  Uncharacterized protein from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)

Seq: 651 a.a.

Struc: 637 a.a.

Enzyme reactions

• Enzyme class: E.C.1.17.4.2 - ribonucleoside-triphosphate reductase (thioredoxin).
• Reaction: a 2'-deoxyribonucleoside 5'-triphosphate + [thioredoxin]-disulfide + H2O = a ribonucleoside 5'-triphosphate + [thioredoxin]-dithiol
• Cofactor: Adenosylcob(III)alamin

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

reference

DOI no: 10.1073/pnas.1414396111

Proc Natl Acad Sci U S A 111:E3756 (2014)

PubMed id: 25157154

The class III ribonucleotide reductase from Neisseria bacilliformis can utilize thioredoxin as a reductant.

Y.Wei, M.A.Funk, L.A.Rosado, J.Baek, C.L.Drennan, J.Stubbe.

ABSTRACT

The class III anaerobic ribonucleotide reductases (RNRs) studied to date couple the reduction of ribonucleotides to deoxynucleotides with the oxidation of formate to CO2. Here we report the cloning and heterologous expression of the Neisseria bacilliformis class III RNR and show that it can catalyze nucleotide reduction using the ubiquitous thioredoxin/thioredoxin reductase/NADPH system. We present a structural model based on a crystal structure of the homologous Thermotoga maritima class III RNR, showing its architecture and the position of conserved residues in the active site. Phylogenetic studies suggest that this form of class III RNR is present in bacteria and archaea that carry out diverse types of anaerobic metabolism.