1FI2

CRYSTAL STRUCTURE OF GERMIN (OXALATE OXIDASE)

Summary for 1FI2

• Entry DOI: 10.2210/pdb1fi2/pdb
• Related: 2PHL
• Descriptor: OXALATE OXIDASE, MANGANESE (II) ION (3 entities in total)
• Functional Keywords: beta-jellyroll, oxidoreductase
• Biological source: Hordeum vulgare
• Cellular location: Secreted, extracellular space, apoplast (By similarity): P45850
• Total number of polymer chains: 1
• Total formula weight: 21292.11

Authors

Woo, E.J.,Dunwell, J.M.,Goodenough, P.W.,Marvier, A.C.,Pickersgill, R.W. (deposition date: 2000-08-03, release date: 2001-05-01, Last modification date: 2024-11-13)

Primary citation

Woo, E.J.,Dunwell, J.M.,Goodenough, P.W.,Marvier, A.C.,Pickersgill, R.W.
Germin is a manganese containing homohexamer with oxalate oxidase and superoxide dismutase activities.
Nat.Struct.Biol., 7:1036-1040, 2000

PubMed Abstract: 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.

PubMed: 11062559
DOI: 10.1038/80954

Experimental method

X-RAY DIFFRACTION (1.6 Å)