5dip: Difference between revisions
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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 with sequence from [https://en.wikipedia.org/wiki/Legionella_pneumophila Legionella pneumophila]. 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 [https://proteopedia.org/fgij/fg.htm?mol=5DIP FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.097Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></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=5dip FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dip OCA], [https://pdbe.org/5dip PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dip RCSB], [https://www.ebi.ac.uk/pdbsum/5dip PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dip ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q5ZYG6_LEGPH Q5ZYG6_LEGPH] | |||
<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> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5dip" style="background-color:#fffaf0;"></div> | ||
[[Category: Ge | == References == | ||
[[Category: | <references/> | ||
[[Category: Zhang | __TOC__ | ||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Legionella pneumophila]] | |||
[[Category: Chen X]] | |||
[[Category: Ge H]] | |||
[[Category: Gong X]] | |||
[[Category: Zhang N]] | |||
Latest revision as of 00:43, 29 June 2023
Crystal structure of lpg0406 in reduced form from Legionella pneumophilaCrystal structure of lpg0406 in reduced form from Legionella pneumophila
Structural highlights
FunctionPublication Abstract from PubMedLpg0406, 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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