3X44

Crystal structure of O-ureido-L-serine-bound K43A mutant of O-ureido-L-serine synthase

Summary for 3X44

• Entry DOI: 10.2210/pdb3x44/pdb
• Descriptor: O-ureido-L-serine synthase, (E)-O-(carbamoylamino)-N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-L-serine (3 entities in total)
• Functional Keywords: d-cycloserine, type ii plp enzyme, synthase, transferase
• Biological source: Streptomyces lavendulae
• Total number of polymer chains: 2
• Total formula weight: 72069.12

Authors

Matoba, Y.,Uda, N.,Oda, K.,Sugiyama, M. (deposition date: 2015-03-13, release date: 2015-07-29, Last modification date: 2024-05-29)

Primary citation

Uda, N.,Matoba, Y.,Oda, K.,Kumagai, T.,Sugiyama, M.
The structural and mutational analyses of O-ureido-L-serine synthase necessary for D-cycloserine biosynthesis.
Febs J., 282:3929-3944, 2015

PubMed Abstract: We have recently been successful in cloning a gene cluster necessary for the biosynthesis of D-cycloserine (D-CS) from D-CS-producing Streptomyces lavendulae ATCC11924. Although dcsD, one of the ORFs located on the gene cluster, encodes a protein homologous to O-acetylserine sulfhydrylase that synthesizes L-cysteine using O-acetyl-L-serine together with sulfide, it functions to form O-ureido-L-serine as a D-CS biosynthetic intermediate, using O-acetyl-L-serine together with hydroxyurea (HU). In the present study, using crystallographic and mutational studies, three amino acid residues in DcsD that are important for the substrate preference toward HU were determined. We showed that two of the three residues are important for the binding of HU into the substrate-binding pocket. The other residue contributes to the formation of a loose hydrogen-bond network during the catalytic reaction. Information regarding the amino acid residues will be very useful in the design of a new catalyst for synthesizing the β-substituted-L-alanine derivatives.

PubMed: 26207937
DOI: 10.1111/febs.13386

Experimental method

X-RAY DIFFRACTION (1.9 Å)