6EWJ

Putative sugar aminotransferase Spr1654 from Streptococcus pneumoniae, apo-form

6EWJ の概要

• エントリーDOI: 10.2210/pdb6ewj/pdb
• 分子名称: Putative capsular polysaccharide biosynthesis protein (2 entities in total)
• 機能のキーワード: teichoic acid, pneumococcus, sugar aminotransferase, plp, sugar binding protein
• 由来する生物種: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 191281.48

構造登録者

Achour, A.,Sun, R.,Sandalova, T.,Han, X. (登録日: 2017-11-04, 公開日: 2018-05-02, 最終更新日: 2024-01-17)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.9 Å)