Insights into the Alkyl Peroxide Reduction Pathway of Xanthomonas campestris Bacterioferritin Comigratory Protein from the Trapped Intermediate–Ligand Complex Structures

Liao, S. J.; Yang, Chih‐Yung; Chin, Ko‐Hsin; Wang, Andrew H.‐J.; Chou, Shan‐Ho

doi:10.1016/j.jmb.2009.05.030

Cited by 27 publications

(42 citation statements)

References 42 publications

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“…6E). The b-hairpin between a4 and b6 is longer in the structures from XcBCP and is thought to play a part in regulating substrate channel accessibility (49). The fact that a different local unfolding structural transition can occur for Prxs with the same C R position supports the hypothesis that the C R positions independently evolved multiple times during the divergence of the Prx family.…”

Section: Subfamily Bcpmentioning

confidence: 96%

“…Although Cys 174 has been identified as the primary C R (27,46), Cys 176 is able to substitute as a C R when Cys 174 has been mutated, retaining *30% of the activity of the wild-type AhpC (46). Similar mechanistic flexibility with lowered catalytic rates has been observed for other C R mutants, although the alternate C R has not been identified [e.g., (17,49)]. …”

mentioning

confidence: 91%

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Structure-based Insights into the Catalytic Power and Conformational Dexterity of Peroxiredoxins

Hall

Nelson²,

Poole³

et al. 2011

Antioxidants & Redox Signaling

296

406

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Peroxiredoxins (Prxs), some of nature's dominant peroxidases, use a conserved Cys residue to reduce peroxides. They are highly expressed in organisms from all kingdoms, and in eukaryotes they participate in hydrogen peroxide signaling. Seventy-two Prx structures have been determined that cover much of the diversity of the family. We review here the current knowledge and show that Prxs can be effectively classified by a structural/evolutionary organization into six subfamilies followed by specification of a 1-Cys or 2-Cys mechanism, and for 2-Cys Prxs, the structural location of the resolving Cys. We visualize the varied catalytic structural transitions and highlight how they differ depending on the location of the resolving Cys. We also review new insights into the question of how Prxs are such effective catalysts: the enzyme activates not only the conserved Cys thiolate but also the peroxide substrate. Moreover, the hydrogen-bonding network created by the four residues conserved in all Prx active sites stabilizes the transition state of the peroxidatic S(N)2 displacement reaction. Strict conservation of the peroxidatic active site along with the variation in structural transitions provides a fascinating picture of how the diverse Prxs function to break down peroxide substrates rapidly.

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Section: Subfamily Bcpmentioning

confidence: 96%

mentioning

confidence: 91%

Structure-based Insights into the Catalytic Power and Conformational Dexterity of Peroxiredoxins

Hall

Nelson²,

Poole³

et al. 2011

Antioxidants & Redox Signaling

296

406

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show abstract

“…Xanthomonas campestris PrxQ ( Xc PrxQ), from an economically important plant pathogen (Leyns et al 1984), is 160-residues long and has relevance for drug design (Myler et al 2009) as it is representative of PrxQs from various genera of human pathogens such as Burkholderia (63% sequence identity), Helicobacter (46%), Cryptosporidium (42%), Toxoplasma (41%), Mycobacterium (40%), and Acanthamoeba (38%). Also, high resolution crystal structures for the disulfide (LU) conformation and the pseudo-dithiol (FF) conformation (Cys→Ser double variant) show that the transition from FF to LU involves a substantial unfolding of helix-3 (Liao et al 2009). With plans to directly measure how redox state, mutations, and post-translational modifications modulate the enzyme’s structure and dynamics, and to enable chemical shift perturbation studies of ligand binding (e.g.…”

Section: Biological Contextmentioning

confidence: 99%

Backbone chemical shift assignments for Xanthomonas campestris peroxiredoxin Q in the reduced and oxidized states: a dramatic change in backbone dynamics

et al. 2015

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Peroxiredoxins (Prx) are ubiquitous enzymes that reduce peroxides as part of antioxidant defenses and redox signaling. While Prx catalytic activity and sensitivity to hyperoxidative inactivation depend on their dynamic properties, there are few examples where their dynamics has been characterized by NMR spectroscopy. Here, we provide a foundation for studies of the solution properties of peroxiredoxin Q from the plant pathogen Xanthomonas campestris (XcPrxQ) by assigning the observable 1 H N , 15 N, 13 C α , 13 C β , and 13 C′ chemical shifts for both the reduced (dithiol) and oxidized (disulfide) states. In the reduced state, most of the backbone amide resonances (149/152, 98%) can be assigned in the XcPrxQ 1 H-15 N HSQC spectrum. In contrast, a remarkable 51% (77) of these amide resonances are not visible in the 1 H-15 N HSQC spectrum of the disulfide state of the enzyme, indicating a substantial change in backbone dynamics associated with the formation of an intramolecular C48-C84 disulfide bond.

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“…The PrxQ subfamily includes both 2-Cys and 1-Cys Prxs (257). For the 2-Cys members, the common location for C R is in helix a2, five residues after C P ; however, about 7% of the subfamily have C R in helix a3 (147,183).…”

mentioning

confidence: 99%

Peroxiredoxins in Parasites

Gretes

Poole²,

Karplus³

2012

Antioxidants & Redox Signaling

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Insights into the Alkyl Peroxide Reduction Pathway of Xanthomonas campestris Bacterioferritin Comigratory Protein from the Trapped Intermediate–Ligand Complex Structures

Cited by 27 publications

References 42 publications

Structure-based Insights into the Catalytic Power and Conformational Dexterity of Peroxiredoxins

Structure-based Insights into the Catalytic Power and Conformational Dexterity of Peroxiredoxins

Backbone chemical shift assignments for Xanthomonas campestris peroxiredoxin Q in the reduced and oxidized states: a dramatic change in backbone dynamics

Peroxiredoxins in Parasites

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