1N8J

Crystal Structure of AhpC with Active Site Cysteine mutated to Serine (C46S)

Summary for 1N8J

• Entry DOI: 10.2210/pdb1n8j/pdb
• Related: 1KYG
• Descriptor: Alkyl hydroperoxide reductase C22 protein (2 entities in total)
• Functional Keywords: ahpc, peroxiredoxin, decamer, antioxidant, peroxidase, alkylhydroperoxide reductase, ahpf, oxidoreductase
• Biological source: Salmonella typhimurium
• Total number of polymer chains: 20
• Total formula weight: 412502.46

Authors

Wood, Z.A.,Poole, L.B.,Karplus, P.A. (deposition date: 2002-11-20, release date: 2003-04-29, Last modification date: 2023-08-16)

Primary citation

Wood, Z.A.,Poole, L.B.,Karplus, P.A.
Peroxiredoxin Evolution and the Regulation of Hydrogen Peroxide Signaling
Science, 300:650-653, 2003

PubMed Abstract: Eukaryotic 2-Cys peroxiredoxins (2-Cys Prxs) not only act as antioxidants, but also appear to regulate hydrogen peroxide-mediated signal transduction. We show that bacterial 2-Cys Prxs are much less sensitive to oxidative inactivation than are eukaryotic 2-Cys Prxs. By identifying two sequence motifs unique to the sensitive 2-Cys Prxs and comparing the crystal structure of a bacterial 2-Cys Prx at 2.2 angstrom resolution with other Prx structures, we define the structural origins of sensitivity. We suggest this adaptation allows 2-Cys Prxs to act as floodgates, keeping resting levels of hydrogen peroxide low, while permitting higher levels during signal transduction.

PubMed: 12714747
DOI: 10.1126/science.1080405

Experimental method

X-RAY DIFFRACTION (2.17 Å)