Bacterioferritin comigratory protein

From Proteopedia

proteopedia linkproteopedia link

spinqualitylabelsall models Caption for this structure Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Contents 1 Function 2 Disease 3 Relevance 4 Structural highlights Function Bacterioferritin comigratory protein or Bacterioferritin comigratory protein peroxiredoxin or thiol peroxidase or peroxiredoxin Q(BCP) is part of the peroxiredoxin family of proteins. BCP is important in hydrogen peroxide resistance, nodulation and nitrogen fixation in bacteria[1]. BCP active site Cys is stabilized as a reactive cys-thiolate and attacks a bound hydrogen peroxide to form Cys-sulfenate and water[2]. Disease Relevance BCP has defensive role against peroxide-mediated cell killing and protects supercoiled DNA against oxidative damage[3]. Structural highlights

3D structures of bacterioferritin comigratory protein

Updated on 16-April-2020

2cx4, 2cx3, 4gqf - BCP - Aeropyrum pernix
3gkk, 5iiz, 5iox - XcBCP- Xanthomonas campestris
5io2, 5iph - XcBCP (mutant)
3gkn - XcBCP (mutant) + naphthalenedisulfonic acid
5im9 - XcBCP + S-hydroxycysteine
5imv, 5imd - XcBCP + formate + cysteinesulfonic acid
5ima, 5imc - XcBCP + formate + S-hydroxycysteine
3gkm - XcBCP (mutant) + formate
5ipg, 5iow, 5io0 - XcBCP + sulfinoalanine + S-hydroxycysteine
5imf, 5iny, 5imz - XcBCP + formate + sulfinoalanine + S-hydroxycysteine
3drn - SsBCP1 (mutant) - Sulfolobus solfataricus
3hjp - SsBCP4 (mutant)
3ixr - BCP (mutant) - Xylella fastidiosas

References

1. ↑ Liu X, Qiu W, Rao B, Cao Y, Fang X, Yang J, Jiang G, Zhong Z, Zhu J. Bacterioferritin comigratory protein is important in hydrogen peroxide resistance, nodulation, and nitrogen fixation in Azorhizobium caulinodans. Arch Microbiol. 2019 Aug;201(6):823-831. doi: 10.1007/s00203-019-01654-8. Epub, 2019 Apr 5. PMID:30953092 doi:http://dx.doi.org/10.1007/s00203-019-01654-8
2. ↑ Perkins A, Parsonage D, Nelson KJ, Ogba OM, Cheong PH, Poole LB, Karplus PA. Peroxiredoxin Catalysis at Atomic Resolution. Structure. 2016 Sep 1. pii: S0969-2126(16)30223-4. doi:, 10.1016/j.str.2016.07.012. PMID:27594682 doi:http://dx.doi.org/10.1016/j.str.2016.07.012
3. ↑ Singh A, Kumar N, Tomar PPS, Bhose S, Ghosh DK, Roy P, Sharma AK. Characterization of a bacterioferritin comigratory protein family 1-Cys peroxiredoxin from Candidatus Liberibacter asiaticus. Protoplasma. 2017 Jul;254(4):1675-1691. doi: 10.1007/s00709-016-1062-z. Epub 2016, Dec 16. PMID:27987036 doi:http://dx.doi.org/10.1007/s00709-016-1062-z