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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Crystal structure and statistical coupling analysis of highly glycosylated peroxidase from royal palm tree (Roystonea regia)

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Watanabe, Leandra [1] ; de Moura, Patricia Ribeiro [1] ; Bleicher, Lucas [1] ; Nascimento, Alessandro S. [1] ; Zamorano, Laura S. [2] ; Calvete, Juan J. [3] ; Sanz, Libia [3] ; Perez, Alicia [3] ; Bursakov, Sergey [4] ; Roig, Manuel G. [2] ; Shnyrov, Valery L. [5] ; Polikarpov, Igor [1]
Total Authors: 12
[1] Univ Sao Paulo, Inst Fis Sao Carlos, Dept Fis & Informat, BR-13566590 Sao Carlos, SP - Brazil
[2] Univ Salamanca, Dept Quim Fis, Fac Quim, E-37008 Salamanca - Spain
[3] CSIC, Inst Biomed Valencia, Valencia 46010 - Spain
[4] Univ Nova Lisboa, REQUIMTE, Dept Quim, Ctr Quim Fina & Biotecnol, Fac Ciencias & Tecnol, P-2829516 Caparica - Portugal
[5] Univ Salamanca, Fac Biol, Dept Bioquim & Biol Mol, Salamanca 37007 - Spain
Total Affiliations: 5
Document type: Journal article
Source: Journal of Structural Biology; v. 169, n. 2, p. 226-242, Feb. 2010.
Field of knowledge: Biological Sciences - Biophysics
Web of Science Citations: 31

Royal palm tree peroxidase (RPTP) is a very stable enzyme in regards to acidity, temperature, H2O2, and organic solvents. Thus, RPTP is a promising candidate for developing H2O2-sensitive biosensors for diverse applications in industry and analytical chemistry. RPTP belongs to the family of class III secretory plant peroxidases, which include horseradish peroxidase isozyme C, soybean and peanut peroxidases. Here we report the X-ray structure of native RPTP isolated from royal palm tree (Roystonea regia) refined to a resolution of 1.85 Å. RPTP has the same overall folding pattern of the plant peroxidase superfamily, and it contains one heme group and two calcium-binding sites in similar locations. The three-dimensional structure of RPTP was solved for a hydroperoxide complex state, and it revealed a bound 2-(N-morpholino) ethanesulfonic acid molecule (MES) positioned at a putative substrate-binding secondary site. Nine N-glycosylation sites are clearly defined in the RPTP electron-density maps, revealing for the first time conformations of the glycan chains of this highly glycosylated enzyme. Furthermore, statistical coupling analysis (SCA) of the plant peroxidase superfamily was performed. This sequence-based method identified a set of evolutionarily conserved sites that mapped to regions surrounding the heme prosthetic group. The SCA matrix also predicted a set of energetically coupled residues that are involved in the maintenance of the structural folding of plant peroxidases. The combination of crystallographic data and SCA analysis provides information about the key structural elements that could contribute to explaining the unique stability of RPTP. (AU)

FAPESP's process: 06/00182-8 - Structural biophysics of nuclear receptors and related proteins
Grantee:Igor Polikarpov
Support type: Research Projects - Thematic Grants