4qx6: Difference between revisions
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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=4qx6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qx6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4qx6 RCSB], [http://www.ebi.ac.uk/pdbsum/4qx6 PDBsum]</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=4qx6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qx6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4qx6 RCSB], [http://www.ebi.ac.uk/pdbsum/4qx6 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a conserved cytosolic enzyme, which plays a key role in glycolysis. GAPDH catalyzes the oxidative phosphorylation of D-glyceraldehyde 3-phosphate using NAD or NADP as a cofactor. In addition, GAPDH localized on the surface of some bacteria is thought to be involved in macromolecular interactions and bacterial pathogenesis. GAPDH on the surface of group B streptococcus (GBS) enhances bacterial virulence and is a potential vaccine candidate. Here, the crystal structure of GBS GAPDH from Streptococcus agalactiae in complex with NAD is reported at 2.46 A resolution. Although the overall structure of GBS GAPDH is very similar to those of other GAPDHs, the crystal structure reveals a significant difference in the area spanning residues 294-307, which appears to be more acidic. The amino-acid sequence of this region of GBS GAPDH is also distinct compared with other GAPDHs. This region therefore may be of interest as an immunogen for vaccine development. | |||
Structure of Streptococcus agalactiae glyceraldehyde-3-phosphate dehydrogenase holoenzyme reveals a novel surface.,Ayres CA, Schormann N, Senkovich O, Fry A, Banerjee S, Ulett GC, Chattopadhyay D Acta Crystallogr F Struct Biol Commun. 2014 Oct;70(Pt 10):1333-9. doi:, 10.1107/S2053230X14019517. Epub 2014 Sep 25. PMID:25286935<ref>PMID:25286935</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Ayres, C A | [[Category: Ayres, C A]] | ||
[[Category: Banerjee, S | [[Category: Banerjee, S]] | ||
[[Category: Chattopadhyay, D | [[Category: Chattopadhyay, D]] | ||
[[Category: Schormann, N | [[Category: Schormann, N]] | ||
[[Category: Glycolysis]] | [[Category: Glycolysis]] | ||
[[Category: Nad]] | [[Category: Nad]] | ||
[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||
[[Category: Rossmann fold]] | [[Category: Rossmann fold]] | ||
Revision as of 10:48, 24 December 2014
CRYSTAL STRUCTURE OF GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE FROM STREPTOCOCCUS AGALACTIAE NEM316 at 2.46 ANGSTROM RESOLUTION
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