5dip
From Proteopedia
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| - | ''' | + | ==Crystal structure of lpg0406 in reduced form from Legionella pneumophila== |
| + | <StructureSection load='5dip' size='340' side='right' caption='[[5dip]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5dip]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DIP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DIP FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5dik|5dik]]</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peroxiredoxin Peroxiredoxin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.15 1.11.1.15] </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=5dip FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dip OCA], [http://pdbe.org/5dip PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dip RCSB], [http://www.ebi.ac.uk/pdbsum/5dip PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/A0A0C9P2U2_LEGPN A0A0C9P2U2_LEGPN]] Antioxidant protein with alkyl hydroperoxidase activity. Required for the reduction of the AhpC active site cysteine residues and for the regeneration of the AhpC enzyme activity.[SAAS:SAAS00088543] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Lpg0406, a hypothetical protein from Legionella pneumophila, belongs to carboxymuconolactone decarboxylase (CMD) family. We determined the crystal structure of lpg0406 both in its apo and reduced form. The structures reveal that lpg0406 forms a hexamer and have disulfide exchange properties. The protein has an all-helical fold with a conserved thioredoxin-like active site CXXC motif and a proton relay system similar to that of alkylhydroperoxidase from Mycobacterium tuberculosis (MtAhpD), suggesting that lpg0406 might function as an enzyme with peroxidase activity and involved in antioxidant defense. A comparison of the size and the surface topology of the putative substrate-binding region between lpg0406 and MtAhpD indicates that the two enzymes accommodate the different substrate preferences. The structural findings will enhance understanding of the CMD family protein structure and its various functions. | ||
| - | + | Structure of lpg0406, a carboxymuconolactone decarboxylase family protein possibly involved in antioxidative response from Legionella pneumophila.,Chen X, Hu Y, Yang B, Gong X, Zhang N, Niu L, Wu Y, Ge H Protein Sci. 2015 Sep 24. doi: 10.1002/pro.2811. PMID:26402328<ref>PMID:26402328</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 5dip" style="background-color:#fffaf0;"></div> | |
| - | [[Category: | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Peroxiredoxin]] | ||
| + | [[Category: Chen, X]] | ||
| + | [[Category: Ge, H]] | ||
[[Category: Gong, X]] | [[Category: Gong, X]] | ||
| - | [[Category: Ge, H]] | ||
| - | [[Category: Chen, X]] | ||
[[Category: Zhang, N]] | [[Category: Zhang, N]] | ||
| + | [[Category: Alkylhydroperoxidase]] | ||
| + | [[Category: Oxidoreductase]] | ||
Revision as of 03:51, 16 October 2015
Crystal structure of lpg0406 in reduced form from Legionella pneumophila
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