6fzh

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'''Unreleased structure'''
 
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The entry 6fzh is ON HOLD until Paper Publication
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==Crystal structure of a streptococcal dehydrogenase at 1.5 Angstroem resolution==
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<StructureSection load='6fzh' size='340' side='right'caption='[[6fzh]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6fzh]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FZH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6FZH FirstGlance]. <br>
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</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>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glyceraldehyde-3-phosphate_dehydrogenase_(phosphorylating) Glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.12 1.2.1.12] </span></td></tr>
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<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=6fzh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fzh OCA], [http://pdbe.org/6fzh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6fzh RCSB], [http://www.ebi.ac.uk/pdbsum/6fzh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6fzh ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/G3P_STRP8 G3P_STRP8]] Catalyzes the oxidative phosphorylation of glyceraldehyde 3-phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor NAD. The first reaction step involves the formation of a hemiacetal intermediate between G3P and a cysteine residue, and this hemiacetal intermediate is then oxidized to a thioester, with concomitant reduction of NAD to NADH. The reduced NADH is then exchanged with the second NAD, and the thioester is attacked by a nucleophilic inorganic phosphate to produce BPG.[UniProtKB:P00362]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The 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.
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Authors:
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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<ref>PMID:28443070</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 6fzh" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Alberti, S]]
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[[Category: Cordoba, S Rodriguez de]]
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[[Category: Fernandez, F J]]
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[[Category: Franco-Hidalgo, V]]
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[[Category: Gomez, S]]
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[[Category: Gonzalez-Alsina, A]]
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[[Category: Melchor-Tafur, C]]
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[[Category: Querol-Garcia, J]]
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[[Category: Sanchez-Barron, G]]
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[[Category: Subias, M]]
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[[Category: Vega, M C]]
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[[Category: Anacardic acid]]
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[[Category: C3]]
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[[Category: C3a]]
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[[Category: C5a]]
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[[Category: Complement]]
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[[Category: Curcumin]]
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[[Category: Dehydrogenase]]
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[[Category: Gapdh]]
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[[Category: Nad]]
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[[Category: Oxidoreductase]]
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[[Category: Streptococcus pyogene]]

Revision as of 06:35, 27 March 2019

Crystal structure of a streptococcal dehydrogenase at 1.5 Angstroem resolution

PDB ID 6fzh

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