Structure of Streptococcus agalactiae glyceraldehyde-3-phosphate dehydrogenase holoenzyme reveals a novel surface

Chapelle A Ayres; Norbert Schormann; Olga Senkovich; Alexandra Fry; Surajit Banerjee; Glen C Ulett; Debasish Chattopadhyay

doi:10.1107/S2053230X14019517

Structure of Streptococcus agalactiae glyceraldehyde-3-phosphate dehydrogenase holoenzyme reveals a novel surface

Acta Crystallogr F Struct Biol Commun. 2014 Oct;70(Pt 10):1333-9. doi: 10.1107/S2053230X14019517. Epub 2014 Sep 25.

Authors

Chapelle A Ayres¹, Norbert Schormann², Olga Senkovich³, Alexandra Fry¹, Surajit Banerjee⁴, Glen C Ulett⁵, Debasish Chattopadhyay²

Affiliations

¹ Science and Technology Honors Program, University of Alabama at Birmingham, Birmingham, AL 35294, USA.
² Center for Biophysical Sciences and Engineering, University of Alabama at Birmingham, Birmingham, AL 35294, USA.
³ Department of Medicine, University of Alabama at Birmingham, Birmingham, AL 35294, USA.
⁴ Northeastern Collaborative Access Team and Department of Chemistry and Chemical Biology, Cornell University, Argonne, IL 60439, USA.
⁵ School of Medical Science and Griffith Health Institute, Griffith University, QLD 4222, Australia.

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.

Keywords: Streptococcus agalactiae; glyceraldehyde 3-phosphate dehydrogenase.

Publication types

Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

Amino Acid Sequence
Bacterial Proteins / chemistry*
Catalytic Domain
Conserved Sequence
Crystallography, X-Ray
Glyceraldehyde-3-Phosphate Dehydrogenases / chemistry*
Models, Molecular
Molecular Sequence Data
NAD / chemistry
Protein Binding
Protein Structure, Quaternary
Streptococcus agalactiae / enzymology*
Structural Homology, Protein
Surface Properties

Substances

Bacterial Proteins
NAD
Glyceraldehyde-3-Phosphate Dehydrogenases

Associated data

PDB/4QX6

Grants and funding

P41 GM103403/GM/NIGMS NIH HHS/United States