1fi2
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(New page: 200px<br /><applet load="1fi2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fi2, resolution 1.6Å" /> '''CRYSTAL STRUCTURE OF ...)
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Revision as of 12:49, 20 November 2007
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CRYSTAL STRUCTURE OF GERMIN (OXALATE OXIDASE)
Overview
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.
About this Structure
1FI2 is a Single protein structure of sequence from Hordeum vulgare with MN as ligand. Active as Oxalate oxidase, with EC number 1.2.3.4 Full crystallographic information is available from OCA.
Reference
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
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