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Crystal Structures of Group B Streptococcus Glyceraldehyde-3-Phosphate Dehydrogenase: Apo-Form, Binary and Ternary Complexes.

Schormann N, Ayres CA, Fry A, Green TJ, Banerjee S, Ulett GC, Chattopadhyay D
PLoS One 11 e0165917 (2016)
Related entries: 5jy6, 5jye, 5jyf

Cited: 8 times
EuropePMC logo PMID: 27875551

Abstract

Glyceraldehyde 3-phosphate dehydrogenase or GAPDH is an evolutionarily conserved glycolytic enzyme. It catalyzes the two step oxidative phosphorylation of D-glyceraldehyde 3-phosphate into 1,3-bisphosphoglycerate using inorganic phosphate and NAD+ as cofactor. GAPDH of Group B Streptococcus is a major virulence factor and a potential vaccine candidate. Moreover, since GAPDH activity is essential for bacterial growth it may serve as a possible drug target. Crystal structures of Group B Streptococcus GAPDH in the apo-form, two different binary complexes and the ternary complex are described here. The two binary complexes contained NAD+ bound to 2 (mixed-holo) or 4 (holo) subunits of the tetrameric protein. The structure of the mixed-holo complex reveals the effects of NAD+ binding on the conformation of the protein. In the ternary complex, the phosphate group of the substrate was bound to the new Pi site in all four subunits. Comparison with the structure of human GAPDH showed several differences near the adenosyl binding pocket in Group B Streptococcus GAPDH. The structures also reveal at least three surface-exposed areas that differ in amino acid sequence compared to the corresponding areas of human GAPDH.

Articles - 5jya mentioned but not cited (3)

  1. Crystal Structures of Group B Streptococcus Glyceraldehyde-3-Phosphate Dehydrogenase: Apo-Form, Binary and Ternary Complexes. Schormann N, Ayres CA, Fry A, Green TJ, Banerjee S, Ulett GC, Chattopadhyay D. PLoS One 11 e0165917 (2016)
  2. Chlamydia trachomatis glyceraldehyde 3-phosphate dehydrogenase: Enzyme kinetics, high-resolution crystal structure, and plasminogen binding. Schormann N, Campos J, Motamed R, Hayden KL, Gould JR, Green TJ, Senkovich O, Banerjee S, Ulett GC, Chattopadhyay D. Protein Sci 29 2446-2458 (2020)
  3. High-resolution crystal structure of Streptococcus agalactiae glyceraldehyde-3-phosphate dehydrogenase. Zhou K, Fan X, Li Y, Zhang C, Jin T. Acta Crystallogr F Struct Biol Commun 74 236-244 (2018)


Articles citing this publication (5)

  1. Research Support, Non-U.S. Gov't CHARMM-GUI ligand reader and modeler for CHARMM force field generation of small molecules. Kim S, Lee J, Jo S, Brooks CL, Lee HS, Im W. J Comput Chem 38 1879-1886 (2017)
  2. Epitopes identified in GAPDH from Clostridium difficile recognized as common antigens with potential autoimmunizing properties. Razim A, Pacyga K, Aptekorz M, Martirosian G, Szuba A, Pawlak-Adamska E, Brzychczy-Włoch M, Myc A, Gamian A, Górska S. Sci Rep 8 13946 (2018)
  3. Porphyromonas gingivalis HmuY and Streptococcus gordonii GAPDH-Novel Heme Acquisition Strategy in the Oral Microbiome. Ślęzak P, Śmiga M, Smalley JW, Siemińska K, Olczak T. Int J Mol Sci 21 E4150 (2020)
  4. Structures of glyceraldehyde 3-phosphate dehydrogenase in Neisseria gonorrhoeae and Chlamydia trachomatis. Barrett KF, Dranow DM, Phan IQ, Michaels SA, Shaheen S, Navaluna ED, Craig JK, Tillery LM, Choi R, Edwards TE, Conrady DG, Abendroth J, Horanyi PS, Lorimer DD, Van Voorhis WC, Zhang Z, Barrett LK, Subramanian S, Staker B, Fan E, Myler PJ, Soge OO, Hybiske K, Ojo KK. Protein Sci 29 768-778 (2020)
  5. Streptococcus agalactiae glyceraldehyde-3-phosphate dehydrogenase (GAPDH) elicits multiple cytokines from human cells and has a minor effect on bacterial persistence in the murine female reproductive tract. Sullivan MJ, Goh KGK, Thapa R, Chattopadhyay D, Ipe DS, Duell BL, Katupitiya L, Gosling D, Acharya D, Ulett GC. Virulence 12 3015-3027 (2021)


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