5IPH

Xanthomonas campestris Peroxiredoxin Q - C84S mutant

Summary for 5IPH

• Entry DOI: 10.2210/pdb5iph/pdb
• Related: 5IIZ 5IM9 5IMA 5IMC 5IMD 5IMF 5IMV 5IMZ 5INY 5IO0 5IO2 5IOW 5IOX 5IPG
• Descriptor: Bacterioferritin comigratory protein, SODIUM ION (3 entities in total)
• Functional Keywords: prxq, bcp, peroxidase, redox, oxidoreductase
• Biological source: Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25)
• Total number of polymer chains: 1
• Total formula weight: 17201.53

Authors

Perkins, A.,Parsonage, D.,Nelson, K.J.,Poole, L.B.,Karplus, A. (deposition date: 2016-03-09, release date: 2016-09-21, Last modification date: 2024-10-30)

Primary citation

Perkins, A.,Parsonage, D.,Nelson, K.J.,Ogba, O.M.,Cheong, P.H.,Poole, L.B.,Karplus, P.A.
Peroxiredoxin Catalysis at Atomic Resolution.
Structure, 24:1668-1678, 2016

PubMed Abstract: Peroxiredoxins (Prxs) are ubiquitous cysteine-based peroxidases that guard cells against oxidative damage, are virulence factors for pathogens, and are involved in eukaryotic redox regulatory pathways. We have analyzed catalytically active crystals to capture atomic resolution snapshots of a PrxQ subfamily enzyme (from Xanthomonas campestris) proceeding through thiolate, sulfenate, and sulfinate species. These analyses provide structures of unprecedented accuracy for seeding theoretical studies, and reveal conformational intermediates giving insight into the reaction pathway. Based on a highly non-standard geometry seen for the sulfenate intermediate, we infer that the sulfenate formation itself can strongly promote local unfolding of the active site to enhance productive catalysis. Further, these structures reveal that preventing local unfolding, in this case via crystal contacts, results in facile hyperoxidative inactivation even for Prxs normally resistant to such inactivation. This supports previous proposals that conformation-specific inhibitors may be useful for achieving selective inhibition of Prxs that are drug targets.

PubMed: 27594682
DOI: 10.1016/j.str.2016.07.012

Experimental method

X-RAY DIFFRACTION (1.3 Å)