3B1F

Crystal structure of prephenate dehydrogenase from Streptococcus mutans

Summary for 3B1F

• Entry DOI: 10.2210/pdb3b1f/pdb
• Descriptor: Putative prephenate dehydrogenase, NICOTINAMIDE-ADENINE-DINUCLEOTIDE (3 entities in total)
• Functional Keywords: enzyme, prephenate, 4-hydroxyphenylpyruvate, oxidative decarboxylation pathway, tyrosine biosynthesis, oxidoreductase
• Biological source: Streptococcus mutans
• Total number of polymer chains: 1
• Total formula weight: 33261.49

Authors

Ku, H.K.,Do, N.H.,Song, J.S.,Choi, S.,Shin, M.H.,Kim, K.J.,Lee, S.J. (deposition date: 2011-07-02, release date: 2011-10-26, Last modification date: 2024-10-23)

Primary citation

Ku, H.K.,Do, N.H.,Song, J.S.,Choi, S.,Yeon, S.H.,Shin, M.H.,Kim, K.J.,Park, S.R.,Park, I.Y.,Kim, S.K.,Lee, S.J.
Crystal structure of prephenate dehydrogenase from Streptococcus mutans.
Int.J.Biol.Macromol., 49:761-766, 2011

PubMed Abstract: Prephenate dehydrogenase (PDH) is a bacterial enzyme that catalyzes conversion of prephenate to 4-hydroxyphenylpyruvate through the oxidative decarboxylation pathway for tyrosine biosynthesis. This enzymatic pathway exists in prokaryotes but is absent in mammals, indicating that it is a potential target for the development of new antibiotics. The crystal structure of PDH from Streptococcus mutans in a complex with NAD(+) shows that the enzyme exists as a homo-dimer, each monomer consisting of two domains, a modified nucleotide binding N-terminal domain and a helical prephenate C-terminal binding domain. The latter is the dimerization domain. A structural comparison of PDHs from mesophilic S. mutans and thermophilic Aquifex aeolicus showed differences in the long loop between β6 and β7, which may be a reason for the high K(m) values of PDH from Streptococcus mutans.

PubMed: 21798280
DOI: 10.1016/j.ijbiomac.2011.07.009

Experimental method

X-RAY DIFFRACTION (2.1 Å)