1NM3

Crystal structure of Heamophilus influenza hybrid-Prx5

Summary for 1NM3

• Entry DOI: 10.2210/pdb1nm3/pdb
• Descriptor: Protein HI0572, SULFATE ION (2 entities in total)
• Functional Keywords: hybrid, peroxiredoxin, glutaredoxin, electron transport
• Biological source: Haemophilus influenzae
• Total number of polymer chains: 2
• Total formula weight: 54683.63

Authors

Kim, S.J.,Woo, J.R.,Hwang, Y.S.,Jeong, D.G.,Shin, D.H.,Kim, K.H.,Ryu, S.E. (deposition date: 2003-01-08, release date: 2003-03-25, Last modification date: 2011-07-13)

Primary citation

Kim, S.J.,Woo, J.R.,Hwang, Y.S.,Jeong, D.G.,Shin, D.H.,Kim, K.,Ryu, S.E.
The Tetrameric Structure of Haemophilus influenza Hybrid Prx5 Reveals Interactions between Electron Donor and Acceptor Proteins.
J.Biol.Chem., 278:10790-10798, 2003

PubMed Abstract: Cellular redox control is often mediated by oxidation and reduction of cysteine residues in the redox-sensitive proteins, where thioredoxin and glutaredoxin (Grx) play as electron donors for the oxidized proteins. Despite the importance of protein-protein interactions between the electron donor and acceptor proteins, there has been no structural information for the interaction of thioredoxin or Grx with natural target proteins. Here, we present the crystal structure of a novel Haemophilus influenza peroxiredoxin (Prx) hybrid Prx5 determined at 2.8-A resolution. The structure reveals that hybrid Prx5 forms a tightly associated tetramer where active sites of Prx and Grx domains of different monomers interact with each other. The Prx-Grx interface comprises specific charge interactions surrounded by weak interactions, providing insight into the target recognition mechanism of Grx. The tetrameric structure also exhibits a flexible active site and alternative Prx-Grx interactions, which appear to facilitate the electron transfer from Grx to Prx domain. Differences of electron donor binding surfaces in Prx proteins revealed by an analysis based on the structural information explain the electron donor specificities of various Prx proteins.

PubMed: 12529327
DOI: 10.1074/jbc.M209553200

Experimental method

X-RAY DIFFRACTION (2.8 Å)