3fe5
From Proteopedia
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| - | [[ | + | ==Crystal structure of 3-hydroxyanthranilate 3,4-dioxygenase from bovine kidney== |
| + | <StructureSection load='3fe5' size='340' side='right' caption='[[3fe5]], [[Resolution|resolution]] 2.51Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3fe5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FE5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3FE5 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr> | ||
| + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2qnk|2qnk]], [[1zvf|1zvf]], [[1yfy|1yfy]]</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/3-hydroxyanthranilate_3,4-dioxygenase 3-hydroxyanthranilate 3,4-dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.6 1.13.11.6] </span></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3fe5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fe5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3fe5 RCSB], [http://www.ebi.ac.uk/pdbsum/3fe5 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fe/3fe5_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 3-Hydroxyanthranilate 3,4-dioxygenase, the enzyme that catalyzes the conversion of 3-hydroxyanthranilate to quinolinic acid, has been extracted and purified from bovine kidney, crystallized and its structure determined at 2.5 A resolution. The enzyme, which crystallizes in the triclinic P1 space group, is a monomer, characterized by the so-called cupin fold. The monomer of the bovine enzyme mimics the dimer present in lower species, such as bacteria and yeast, since it is composed of two domains: one of them is equivalent to one monomer, whilst the second domain corresponds to only a portion of it. The active site consists of an iron ion coordinated by two histidine residues, one glutamate and an external ligand, which has been interpreted as a solvent molecule. It is contained in the N-terminal domain, whilst the function of the C-terminal domain is possibly structural. The catalytic mechanism very likely has been conserved through all species, since the positions of all residues considered relevant for the reaction are present from bacteria to humans. (c) 2009 Wiley Periodicals, Inc. Biopolymers, 2009. | ||
| - | + | Crystal structure of bovine 3-hydroxyanthranilate 3,4-dioxygenase.,Dilovic I, Gliubich F, Malpeli G, Zanotti G, Matkovic-Calogovic D Biopolymers. 2009 Feb 18. PMID:19226621<ref>PMID:19226621</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| - | + | ==See Also== | |
| - | + | *[[Dioxygenase|Dioxygenase]] | |
| - | == | + | == References == |
| - | [[ | + | <references/> |
| - | + | __TOC__ | |
| - | == | + | </StructureSection> |
| - | < | + | |
[[Category: 3-hydroxyanthranilate 3,4-dioxygenase]] | [[Category: 3-hydroxyanthranilate 3,4-dioxygenase]] | ||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
| - | [[Category: Dilovic, I | + | [[Category: Dilovic, I]] |
| - | [[Category: Gliubich, F | + | [[Category: Gliubich, F]] |
| - | [[Category: Malpeli, G | + | [[Category: Malpeli, G]] |
| - | [[Category: Matkovic-Calogovic, D | + | [[Category: Matkovic-Calogovic, D]] |
| - | [[Category: Zanotti, G | + | [[Category: Zanotti, G]] |
| - | + | ||
[[Category: Cupin]] | [[Category: Cupin]] | ||
[[Category: Dioxygenase]] | [[Category: Dioxygenase]] | ||
Revision as of 08:58, 26 November 2014
Crystal structure of 3-hydroxyanthranilate 3,4-dioxygenase from bovine kidney
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