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 1.6&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
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[[Image:1fi2.gif|left|200px]]<br /><applet load="1fi2" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1fi2.gif|left|200px]]<br /><applet load="1fi2" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1fi2, resolution 1.6&Aring;" />
caption="1fi2, resolution 1.6&Aring;" />
'''CRYSTAL STRUCTURE OF GERMIN (OXALATE OXIDASE)'''<br />
'''CRYSTAL STRUCTURE OF GERMIN (OXALATE OXIDASE)'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1FI2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Hordeum_vulgare Hordeum vulgare] with MN as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FI2 OCA].
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1FI2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Hordeum_vulgare Hordeum vulgare] with <scene name='pdbligand=MN:'>MN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FI2 OCA].
==Reference==
==Reference==
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[[Category: Oxalate oxidase]]
[[Category: Oxalate oxidase]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Dunwell, J.M.]]
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[[Category: Dunwell, J M.]]
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[[Category: Goodenough, P.W.]]
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[[Category: Goodenough, P W.]]
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[[Category: Marvier, A.C.]]
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[[Category: Marvier, A C.]]
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[[Category: Pickersgill, R.W.]]
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[[Category: Pickersgill, R W.]]
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[[Category: Woo, E.J.]]
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[[Category: Woo, E J.]]
[[Category: MN]]
[[Category: MN]]
[[Category: beta-jellyroll]]
[[Category: beta-jellyroll]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:56:20 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:38:53 2008''

Revision as of 10:38, 21 February 2008


1fi2, resolution 1.6Å

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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 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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