Skip to main content
padlock icon - secure page this page is secure

The 1.4 Å resolution structure of Paracoccus pantotrophus pseudoazurin

Buy Article:

$52.00 + tax (Refund Policy)

Pseudoazurins are small type 1 copper proteins that are involved in the flow of electrons between various electron donors and acceptors in the bacterial periplasm, mostly under denitrifying conditions. The previously determined structure of Paracoccus pantotrophus pseudoazurin in the oxidized form was improved to a nominal resolution of 1.4 Å, with R and R free values of 0.188 and 0.206, respectively. This high‐resolution structure makes it possible to analyze the interactions between the monomers and the solvent structure in detail. Analysis of the high‐resolution structure revealed the structural regions that are responsible for monomer–monomer recognition during dimer formation and for protein–protein interaction and that are important for partner recognition. The pseudoazurin structure was compared with other structures of various type 1 copper proteins and these were grouped into families according to similarities in their secondary structure; this may be useful in the annotation of copper proteins in newly sequenced genomes and in the identification of novel copper proteins.
No References
No Citations
No Supplementary Data
No Article Media
No Metrics

Keywords: Paracoccus pantotrophus; copper proteins; electron transfer; pseudoazurin; type 1 blue copper protein family

Document Type: Research Article

Affiliations: REQUIMTE, Centro de Química Fina e Biotecnologia, Departamento de Química, Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa, 2829-516 Caparica, Portugal

Publication date: June 1, 2010

  • Access Key
  • Free content
  • Partial Free content
  • New content
  • Open access content
  • Partial Open access content
  • Subscribed content
  • Partial Subscribed content
  • Free trial content
Cookie Policy
X
Cookie Policy
Ingenta Connect website makes use of cookies so as to keep track of data that you have filled in. I am Happy with this Find out more