5FBS

Crystal structure of rifampin phosphotransferase RPH-Lm from Listeria monocytogenes in complex with ADP and magnesium

5FBS の概要

• エントリーDOI: 10.2210/pdb5fbs/pdb
• 関連するPDBエントリー: 5FBT 5FBU
• 分子名称: Phosphoenolpyruvate synthase, MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: antibiotic resistance, rifamycins, rifampin, phosphotransferase, atp grasp domain, phosphohistidine domain, structural genomics, center for structural genomics of infectious diseases, csgid, transferase
• 由来する生物種: Listeria monocytogenes serotype 4b str. F2365
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 97443.16

構造登録者

Stogios, P.J.,Wawrzak, Z.,Skarina, T.,Yim, V.,Savchenko, A.,Anderson, W.F.,Center for Structural Genomics of Infectious Diseases (CSGID) (登録日: 2015-12-14, 公開日: 2016-01-13, 最終更新日: 2023-09-27)

主引用文献

Stogios, P.J.,Cox, G.,Spanogiannopoulos, P.,Pillon, M.C.,Waglechner, N.,Skarina, T.,Koteva, K.,Guarne, A.,Savchenko, A.,Wright, G.D.
Rifampin phosphotransferase is an unusual antibiotic resistance kinase.
Nat Commun, 7:11343-11343, 2016

PubMed Abstract: Rifampin (RIF) phosphotransferase (RPH) confers antibiotic resistance by conversion of RIF and ATP, to inactive phospho-RIF, AMP and Pi. Here we present the crystal structure of RPH from Listeria monocytogenes (RPH-Lm), which reveals that the enzyme is comprised of three domains: two substrate-binding domains (ATP-grasp and RIF-binding domains); and a smaller phosphate-carrying His swivel domain. Using solution small-angle X-ray scattering and mutagenesis, we reveal a mechanism where the swivel domain transits between the spatially distinct substrate-binding sites during catalysis. RPHs are previously uncharacterized dikinases that are widespread in environmental and pathogenic bacteria. These enzymes are members of a large unexplored group of bacterial enzymes with substrate affinities that have yet to be fully explored. Such an enzymatically complex mechanism of antibiotic resistance augments the spectrum of strategies used by bacteria to evade antimicrobial compounds.

PubMed: 27103605
DOI: 10.1038/ncomms11343

実験手法

X-RAY DIFFRACTION (2.59 Å)