1fi2

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1fi2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Hordeum_vulgare Hordeum vulgare]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FI2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FI2 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1fi2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Hordeum_vulgare Hordeum vulgare]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FI2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FI2 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2phl|2phl]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Oxalate_oxidase Oxalate oxidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.3.4 1.2.3.4] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fi2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fi2 OCA], [https://pdbe.org/1fi2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fi2 RCSB], [https://www.ebi.ac.uk/pdbsum/1fi2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fi2 ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fi2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fi2 OCA], [https://pdbe.org/1fi2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fi2 RCSB], [https://www.ebi.ac.uk/pdbsum/1fi2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fi2 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/OXO1_HORVU 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.
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[https://www.uniprot.org/uniprot/OXO1_HORVU 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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1fi2 ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1fi2 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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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 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<ref>PMID:11062559</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 1fi2" style="background-color:#fffaf0;"></div>
 
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Hordeum vulgare]]
[[Category: Hordeum vulgare]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Oxalate oxidase]]
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[[Category: Dunwell JM]]
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[[Category: Dunwell, J M]]
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[[Category: Goodenough PW]]
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[[Category: Goodenough, P W]]
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[[Category: Marvier AC]]
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[[Category: Marvier, A C]]
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[[Category: Pickersgill RW]]
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[[Category: Pickersgill, R W]]
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[[Category: Woo EJ]]
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[[Category: Woo, E J]]
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[[Category: Beta-jellyroll]]
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[[Category: Oxidoreductase]]
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Current revision

CRYSTAL STRUCTURE OF GERMIN (OXALATE OXIDASE)

PDB ID 1fi2

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