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Crystal structure analysis of peroxidase from the palm tree Chamaerops excelsa

Bernardes, Amanda and Textor, Larissa C and Santos, Jademilson C and Cuadrado, Nazaret Hidalgo and Kostetsky, Eduard Ya and Roig, Manuel G and Bavro, Vassiliy N and Muniz, João RC and Shnyrov, Valery L and Polikarpov, Igor (2015) 'Crystal structure analysis of peroxidase from the palm tree Chamaerops excelsa.' Biochimie, 111. 58 - 69. ISSN 0300-9084

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Abstract

Palm tree peroxidases are known to be very stable enzymes and the peroxidase from the Chamaerops excelsa (CEP), which has a high pH and thermal stability, is no exception. To date, the structural and molecular events underscoring such biochemical behavior have not been explored in depth. In order to identify the structural characteristics accounting for the high stability of palm tree peroxidases, we solved and refined the X-ray structure of native CEP at a resolution of 2.6 Å. The CEP structure has an overall fold typical of plant peroxidases and confirmed the conservation of characteristic structural elements such as the heme group and calcium ions. At the same time the structure revealed important modifications in the amino acid residues in the vicinity of the exposed heme edge region, involved in substrate binding, that could account for the morphological variations among palm tree peroxidases through the disruption of molecular interactions at the second binding site. These modifications could alleviate the inhibition of enzymatic activity caused by molecular interactions at the latter binding site. Comparing the CEP crystallographic model described here with other publicly available peroxidase structures allowed the identification of a noncovalent homodimer assembly held together by a number of ionic and hydrophobic interactions. We demonstrate, that this dimeric arrangement results in a more stable protein quaternary structure through stabilization of the regions that are highly dynamic in other peroxidases. In addition, we resolved five N-glycosylation sites, which might also contribute to enzyme stability and resistance against proteolytic cleavage.

Item Type: Article
Uncontrolled Keywords: Plant peroxidase, Chamaerops excelsa, Oxidoreductases, Protein crystallography, Protein oligomerization
Subjects: Q Science > QH Natural history > QH301 Biology
Divisions: Faculty of Science and Health > Life Sciences, School of
Depositing User: Jim Jamieson
Date Deposited: 06 Oct 2016 16:17
Last Modified: 28 Jun 2021 13:15
URI: http://repository.essex.ac.uk/id/eprint/17729

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