5ld5: Difference between revisions
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==Crystal structure of a bacterial dehydrogenase at 2.19 Angstroms resolution== | ==Crystal structure of a bacterial dehydrogenase at 2.19 Angstroms resolution== | ||
<StructureSection load='5ld5' size='340' side='right' caption='[[5ld5]], [[Resolution|resolution]] 2.19Å' scene=''> | <StructureSection load='5ld5' size='340' side='right'caption='[[5ld5]], [[Resolution|resolution]] 2.19Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5ld5]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LD5 OCA]. For a <b>guided tour on the structure components</b> use [http:// | <table><tr><td colspan='2'>[[5ld5]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LD5 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5LD5 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=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr> | </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=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5ld5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ld5 OCA], [http://pdbe.org/5ld5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ld5 RCSB], [http://www.ebi.ac.uk/pdbsum/5ld5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ld5 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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</div> | </div> | ||
<div class="pdbe-citations 5ld5" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5ld5" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Glyceraldehyde-3-phosphate dehydrogenase 3D structures|Glyceraldehyde-3-phosphate dehydrogenase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Fernandez, F J]] | [[Category: Fernandez, F J]] | ||
[[Category: Fulla, D]] | [[Category: Fulla, D]] | ||
Revision as of 10:07, 5 August 2020
Crystal structure of a bacterial dehydrogenase at 2.19 Angstroms resolutionCrystal structure of a bacterial dehydrogenase at 2.19 Angstroms resolution
Structural highlights
Publication Abstract from PubMedThe Gram-positive anaerobic human pathogenic bacterium Atopobium vaginae causes most diagnosed cases of bacterial vaginosis as well as opportunistic infections in immunocompromised patients. In addition to its well-established role in carbohydrate metabolism, D-glyceraldehyde-3-phosphate dehydrogenase (GAPDH) from Streptococcus pyogenes and S. pneumoniae have been reported to act as extracellular virulence factors during streptococcal infections. Here, we report the crystal structure of GAPDH from A. vaginae (AvGAPDH) at 2.19 A resolution. The refined model has a crystallographic Rfree of 22.6%. AvGAPDH is a homotetramer wherein each subunit is bound to a nicotinamide adenine dinucleotide (NAD+) molecule. The AvGAPDH enzyme fulfills essential glycolytic as well as moonlight (non-glycolytic) functions, both of which might be targets of chemotherapeutic intervention. We report that AvGAPDH interacts in vitro with the human C5a anaphylatoxin and inhibits C5a-specific granulocyte chemotaxis, thereby suggesting the participation of AvGAPDH in complement-targeted immunoevasion in a context of infection. The availability of high-quality structures of AvGAPDH and other homologous virulence factors from Gram-positive pathogens is critical for drug discovery programs. In this study, sequence and structural differences between AvGAPDH and related bacterial and eukaryotic GAPDH enzymes are reported in an effort to understand how to subvert the immunoevasive properties of GAPDH and evaluate the potential of AvGAPDH as a druggable target. Crystal Structure of Glyceraldehyde-3-Phosphate Dehydrogenase from the Gram-Positive Bacterial Pathogen A. vaginae, an Immunoevasive Factor that Interacts with the Human C5a Anaphylatoxin.,Querol-Garcia J, Fernandez FJ, Marin AV, Gomez S, Fulla D, Melchor-Tafur C, Franco-Hidalgo V, Alberti S, Juanhuix J, Rodriguez de Cordoba S, Regueiro JR, Vega MC Front Microbiol. 2017 Apr 10;8:541. doi: 10.3389/fmicb.2017.00541. eCollection, 2017. PMID:28443070[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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