title: Structure of Streptococcus agalactiae glyceraldehyde-3-phosphate dehydrogenase holoenzyme reveals a novel surface.
abstract: 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 Å 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.
authors.affiliation: Science and Technology Honors Program, University of Alabama at Birmingham, Birmingham, AL 35294, USA.
authors.forename: Chapelle A
authors.initials: CA
authors.lastname: Ayres
authors.affiliation: Center for Biophysical Sciences and Engineering, University of Alabama at Birmingham, Birmingham, AL 35294, USA.
authors.forename: Norbert
authors.initials: N
authors.lastname: Schormann
authors.affiliation: Department of Medicine, University of Alabama at Birmingham, Birmingham, AL 35294, USA.
authors.forename: Olga
authors.initials: O
authors.lastname: Senkovich
authors.affiliation: Science and Technology Honors Program, University of Alabama at Birmingham, Birmingham, AL 35294, USA.
authors.forename: Alexandra
authors.initials: A
authors.lastname: Fry
authors.affiliation: Northeastern Collaborative Access Team and Department of Chemistry and Chemical Biology, Cornell University, Argonne, IL 60439, USA.
authors.forename: Surajit
authors.initials: S
authors.lastname: Banerjee
authors.affiliation: School of Medical Science and Griffith Health Institute, Griffith University, QLD 4222, Australia.
authors.forename: Glen C
authors.initials: GC
authors.lastname: Ulett
authors.affiliation: Center for Biophysical Sciences and Engineering, University of Alabama at Birmingham, Birmingham, AL 35294, USA.
authors.forename: Debasish
authors.initials: D
authors.lastname: Chattopadhyay
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry*; D020134:Catalytic Domain; D017124:Conserved Sequence; D018360:Crystallography, X-Ray; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009243:NAD / Q000737:chemistry; D011485:Protein Binding; D020836:Protein Structure, Quaternary; D013292:Streptococcus agalactiae / Q000201:enzymology*; D040681:Structural Homology, Protein; D013499:Surface Properties
chemical_list: D001426:Bacterial Proteins; D009243:NAD; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases
keywords: Streptococcus agalactiae; glyceraldehyde 3-phosphate dehydrogenase