3MK3

Crystal structure of Lumazine synthase from Salmonella typhimurium LT2

3MK3 の概要

• エントリーDOI: 10.2210/pdb3mk3/pdb
• 分子名称: 6,7-dimethyl-8-ribityllumazine synthase, SULFATE ION (2 entities in total)
• 機能のキーワード: icosahedral, flavodoxin like fold, transferase, dmrl synthase, riboflavin biosynthesis, drug target
• 由来する生物種: Salmonella typhimurium
• タンパク質・核酸の鎖数: 60
• 化学式量合計: 968922.60

構造登録者

Kumar, P.,Singh, M.,Karthikeyan, S. (登録日: 2010-04-14, 公開日: 2011-02-02, 最終更新日: 2023-11-01)

主引用文献

Kumar, P.,Singh, M.,Karthikeyan, S.
Crystal structure analysis of icosahedral lumazine synthase from Salmonella typhimurium, an antibacterial drug target.
Acta Crystallogr.,Sect.D, 67:131-139, 2011

PubMed Abstract: Riboflavin biosynthesis is an essential pathway in bacteria, in contrast to animals, which obtain riboflavin from their diet. Therefore, the enzymes involved in the riboflavin-biosynthesis pathway are potential targets for the development of antibacterial drugs. Lumazine synthase, an enzyme that is involved in the penultimate step of riboflavin biosynthesis, catalyzes the formation of 6,7-dimethyl-8-ribityllumazine from 3,4-dihydroxy-2-butanone 4-phosphate and 5-amino-6-ribitylamino-2,4-(1H,3H)-pyrimidinedione. Lumazine synthase from Salmonella typhimurium (sLS) has been cloned, overexpressed, purified and was crystallized in three forms, each with different crystal packing. The crystal structure of sLS in the monoclinic space group P2(1) has been determined with 60 subunits per asymmetric unit, packed as an icosahedron, at 3.57 Å resolution. Interestingly, sLS contains an N-terminal proline residue (Pro11) which had previously been suggested to disrupt the formation of the icosohedral assembly. In addition, comparison of the structure of sLS with known orthologous lumazine synthase structures allowed identification of the amino-acid residues involved in substrate binding and catalysis. The sLS structure reported here could serve as a starting point for the development of species-specific antibacterial drugs.

PubMed: 21245535
DOI: 10.1107/S0907444910053370

実験手法

X-RAY DIFFRACTION (3.569 Å)