5KH4

Crystal Structure of Steptococcus pneumoniae Undecaprenyl pyrophosphate Synthase (UPPS) with FARNESYL DIPHOSPHATE

5KH4 の概要

• エントリーDOI: 10.2210/pdb5kh4/pdb
• 分子名称: Isoprenyl transferase, FARNESYL DIPHOSPHATE (2 entities in total)
• 機能のキーワード: upps, native, bacterial, undecaprenyl s. pneumoniae, transferase
• 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: 2
• 化学式量合計: 62587.06

構造登録者

Concha, N.O. (登録日: 2016-06-14, 公開日: 2016-07-20, 最終更新日: 2024-03-06)

主引用文献

Concha, N.,Huang, J.,Bai, X.,Benowitz, A.,Brady, P.,Grady, L.C.,Kryn, L.H.,Holmes, D.,Ingraham, K.,Jin, Q.,Pothier Kaushansky, L.,McCloskey, L.,Messer, J.A.,O'Keefe, H.,Patel, A.,Satz, A.L.,Sinnamon, R.H.,Schneck, J.,Skinner, S.R.,Summerfield, J.,Taylor, A.,Taylor, J.D.,Evindar, G.,Stavenger, R.A.
Discovery and Characterization of a Class of Pyrazole Inhibitors of Bacterial Undecaprenyl Pyrophosphate Synthase.
J.Med.Chem., 59:7299-7304, 2016

PubMed Abstract: Undecaprenyl pyrophosphate synthase (UppS) is an essential enzyme in bacterial cell wall synthesis. Here we report the discovery of Staphylococcus aureus UppS inhibitors from an Encoded Library Technology screen and demonstrate binding to the hydrophobic substrate site through cocrystallography studies. The use of bacterial strains with regulated uppS expression and inhibitor resistant mutant studies confirmed that the whole cell activity was the result of UppS inhibition, validating UppS as a druggable antibacterial target.

PubMed: 27379833
DOI: 10.1021/acs.jmedchem.6b00746

実験手法

X-RAY DIFFRACTION (3.2 Å)