6EWQ

Putative sugar aminotransferase Spr1654 from Streptococcus pneumoniae, PLP-form

Summary for 6EWQ

• Entry DOI: 10.2210/pdb6ewq/pdb
• Descriptor: Putative capsular polysaccharide biosynthesis protein, PYRIDOXAL-5'-PHOSPHATE (3 entities in total)
• Functional Keywords: teichoic acid, pneumococcus, sugar aminotransferase, plp, sugar binding protein
• Biological source: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
• Total number of polymer chains: 4
• Total formula weight: 192270.05

Authors

Achour, A.,Sun, R.,Sandalova, T.,Han, X. (deposition date: 2017-11-06, release date: 2018-05-02, Last modification date: 2024-01-17)

Primary citation

Han, X.,Sun, R.,Sandalova, T.,Achour, A.
Structural and functional studies of Spr1654: an essential aminotransferase in teichoic acid biosynthesis inStreptococcus pneumoniae.
Open Biol, 8:-, 2018

PubMed Abstract: Spr1654 from plays a key role in the production of unusual sugars, presumably functioning as a pyridoxal-5'-phosphate (PLP)-dependent aminotransferase. Spr1654 was predicted to catalyse the transferring of amino group to form the amino sugar 2-acetamido-4-amino-2, 4, 6-trideoxygalactose moiety (AATGal), representing a crucial step in biosynthesis of teichoic acids in We have determined the crystal structures of the apo-, PLP- and PMP-bound forms of Spr1654. Spr1654 forms a homodimer, in which each monomer contains one active site. Using spectrophotometry and based on absorbance profiles of PLP- and PMP-formed enzymes, our results indicate that l-glutamate is most likely the preferred amino donor. Structural superposition of the crystal structures of Spr1654 on previously determined structures of other sugar aminotransferases in complex with glutamate and/or UDP-activated sugar allowed us to identify key Spr1654 residues for ligand binding and catalysis. The crystal structures of Spr1654 and in complex with PLP and PMP can direct the future rational design of novel therapeutic compounds against .

PubMed: 29669826
DOI: 10.1098/rsob.170248

Experimental method

X-RAY DIFFRACTION (2.2 Å)