3b1f | pdb_00003b1f

Crystal structure of prephenate dehydrogenase from Streptococcus mutans

spinqualitylabelsall models 3b1f, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3b1f is a 1 chain structure with sequence from Streptococcus mutans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.1Å Ligands: MSE, NAD Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q8DUW0_STRMU Publication Abstract from PubMed 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 beta6 and beta7, which may be a reason for the high K(m) values of PDH from Streptococcus mutans. Crystal structure of prephenate dehydrogenase from Streptococcus mutans.,Ku HK, Do NH, Song JS, Choi S, Yeon SH, Shin MH, Kim KJ, Park SR, Park IY, Kim SK, Lee SJ Int J Biol Macromol. 2011 Nov 1;49(4):761-6. Epub 2011 Jul 20. PMID:21798280 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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