Structural highlights
Function
[OXO1_HORVU] Releases hydrogen peroxide in the apoplast which may be important for cross-linking reactions in the cell wall biochemistry. May play an important role in several aspects of plant growth and defense mechanisms.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Germin is a hydrogen peroxide generating oxalate oxidase with extreme thermal stability; it is involved in the defense against biotic and abiotic stress in plants. The structure, determined at 1.6 A resolution, comprises beta-jellyroll monomers locked into a homohexamer (a trimer of dimers), with extensive surface burial accounting for its remarkable stability. The germin dimer is structurally equivalent to the monomer of the 7S seed storage proteins (vicilins), indicating evolution from a common ancestral protein. A single manganese ion is bound per germin monomer by ligands similar to those of manganese superoxide dismutase (MnSOD). Germin is also shown to have SOD activity and we propose that the defense against extracellular superoxide radicals is an important additional role for germin and related proteins.
Germin is a manganese containing homohexamer with oxalate oxidase and superoxide dismutase activities.,Woo EJ, Dunwell JM, Goodenough PW, Marvier AC, Pickersgill RW Nat Struct Biol. 2000 Nov;7(11):1036-40. PMID:11062559[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Woo EJ, Dunwell JM, Goodenough PW, Marvier AC, Pickersgill RW. Germin is a manganese containing homohexamer with oxalate oxidase and superoxide dismutase activities. Nat Struct Biol. 2000 Nov;7(11):1036-40. PMID:11062559 doi:http://dx.doi.org/10.1038/80954
