1fi2
From Proteopedia
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|PDB= 1fi2 |SIZE=350|CAPTION= <scene name='initialview01'>1fi2</scene>, resolution 1.6Å | |PDB= 1fi2 |SIZE=350|CAPTION= <scene name='initialview01'>1fi2</scene>, resolution 1.6Å | ||
|SITE= | |SITE= | ||
- | |LIGAND= <scene name='pdbligand=MN:MANGANESE (II) ION'>MN</scene> | + | |LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene> |
- | |ACTIVITY= [http://en.wikipedia.org/wiki/Oxalate_oxidase Oxalate oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.3.4 1.2.3.4] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Oxalate_oxidase Oxalate oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.3.4 1.2.3.4] </span> |
|GENE= | |GENE= | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY=[[2phl|2PHL]] | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fi2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fi2 OCA], [http://www.ebi.ac.uk/pdbsum/1fi2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1fi2 RCSB]</span> | ||
}} | }} | ||
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[[Category: Pickersgill, R W.]] | [[Category: Pickersgill, R W.]] | ||
[[Category: Woo, E J.]] | [[Category: Woo, E J.]] | ||
- | [[Category: MN]] | ||
[[Category: beta-jellyroll]] | [[Category: beta-jellyroll]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:23:18 2008'' |
Revision as of 17:23, 30 March 2008
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, resolution 1.6Å | |||||||
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Ligands: | |||||||
Activity: | Oxalate oxidase, with EC number 1.2.3.4 | ||||||
Related: | 2PHL
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Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
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. 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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