Accessibility navigation


Modeling based on the structure of vicilins predicts a histidine cluster in the active site of oxalate oxidase

Gane, P. J., Dunwell, J. ORCID: https://orcid.org/0000-0003-2147-665X and Warwicker, J. (1998) Modeling based on the structure of vicilins predicts a histidine cluster in the active site of oxalate oxidase. Journal of Molecular Evolution, 46 (4). pp. 488-493. ISSN 1432-1432

Full text not archived in this repository.

It is advisable to refer to the publisher's version if you intend to cite from this work. See Guidance on citing.

To link to this item DOI: 10.1007/PL00006329

Abstract/Summary

It is known that germin, which is a marker of the onset of growth in germinating wheat, is an oxalate oxidase, and also that germins possess sequence similarity with legumin and vicilin seed storage proteins. These two pieces of information have been combined in order to generate a 3D model of germin based on the structure of vicilin and to examine the model with regard to a potential oxalate oxidase active site. A cluster of three histidine residues has been located within the conserved beta-barrel structure. While there is a relatively low level of overall sequence similarity between the model and the vicilin structures, the conservation of amino acids important in maintaining the scaffold of the beta-barrel lends confidence to the juxtaposition of the histidine residues. The cluster is similar structurally to those found in copper amine oxidase and other proteins, leading to the suggestion that it defines a metal-binding location within the oxalate oxidase active site. It is also proposed that the structural elements involved in intermolecular interactions in vicilins may play a role in oligomer formation in germin/oxalate oxidase.

Item Type:Article
Refereed:Yes
Divisions:Life Sciences > School of Biological Sciences > Ecology and Evolutionary Biology
ID Code:7958
Publisher:Springer

University Staff: Request a correction | Centaur Editors: Update this record

Page navigation