3ERX
High-resolution structure of Paracoccus pantotrophus pseudoazurin
Summary for 3ERX
| Entry DOI | 10.2210/pdb3erx/pdb |
| Related | 1ADW |
| Descriptor | Pseudoazurin, COPPER (II) ION, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | pseudoazurin, copper protein, paracoccus, high-resolution, electron transport, metal-binding, transport |
| Biological source | Paracoccus pantotrophus (Thiosphaera pantotropha) |
| Cellular location | Periplasm: P80401 |
| Total number of polymer chains | 2 |
| Total formula weight | 27131.74 |
| Authors | Najmudin, S.,Pauleta, S.R.,Moura, I.,Romao, M.J. (deposition date: 2008-10-03, release date: 2009-10-13, Last modification date: 2023-09-06) |
| Primary citation | Najmudin, S.,Pauleta, S.R.,Moura, I.,Romao, M.J. The 1.4 A resolution structure of Paracoccus pantotrophus pseudoazurin. Acta Crystallogr.,Sect.F, 66:627-635, 2010 Cited by PubMed Abstract: 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 A, 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. PubMed: 20516588DOI: 10.1107/S1744309110013989 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.25 Å) |
Structure validation
Download full validation report
