5iow

Xanthomonas campestris Peroxiredoxin Q - Structure FFcumene (Hyperoxidized by cumene hydroperoxide)

spinqualitylabelsall models 5iow, resolution 1.35Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5iow is a 1 chain structure with sequence from Xanthomonas campestris pv. campestris str. ATCC 33913. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.35Å Ligands: ACE, CSD, NA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function BCP_XANCP Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. Publication Abstract from PubMed 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. Peroxiredoxin Catalysis at Atomic Resolution.,Perkins A, Parsonage D, Nelson KJ, Ogba OM, Cheong PH, Poole LB, Karplus PA Structure. 2016 Sep 1. pii: S0969-2126(16)30223-4. doi:, 10.1016/j.str.2016.07.012. PMID:27594682 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Bacterioferritin comigratory protein

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