3F9I

Crystal structure of 3-ketoacyl-(acyl-carrier-protein) reductase Rickettsia prowazekii

3F9I の概要

• エントリーDOI: 10.2210/pdb3f9i/pdb
• 分子名称: 3-oxoacyl-[acyl-carrier-protein] reductase (2 entities in total)
• 機能のキーワード: 3-ketoacyl-(acyl-carrier-protein) reductase, rickettsia, fatty acid biosynthesis, lipid synthesis, nadp, oxidoreductase, structural genomics, seattle structural genomics center for infectious disease, ssgcid
• 由来する生物種: Rickettsia prowazekii
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 53637.98

構造登録者

Seattle Structural Genomics Center for Infectious Disease (SSGCID) (登録日: 2008-11-13, 公開日: 2008-11-25, 最終更新日: 2023-09-06)

主引用文献

Subramanian, S.,Abendroth, J.,Phan, I.Q.,Olsen, C.,Staker, B.L.,Napuli, A.,Van Voorhis, W.C.,Stacy, R.,Myler, P.J.
Structure of 3-ketoacyl-(acyl-carrier-protein) reductase from Rickettsia prowazekii at 2.25 A resolution.
Acta Crystallogr.,Sect.F, 67:1118-1122, 2011

PubMed Abstract: Rickettsia prowazekii, a parasitic Gram-negative bacterium, is in the second-highest biodefense category of pathogens of the National Institute of Allergy and Infectious Diseases, but only a handful of structures have been deposited in the PDB for this bacterium; to date, all of these have been solved by the SSGCID. Owing to its small genome (about 800 protein-coding genes), it relies on the host for many basic biosynthetic processes, hindering the identification of potential antipathogenic drug targets. However, like many bacteria and plants, its metabolism does depend upon the type II fatty-acid synthesis (FAS) pathway for lipogenesis, whereas the predominant form of fatty-acid biosynthesis in humans is via the type I pathway. Here, the structure of the third enzyme in the FAS pathway, 3-ketoacyl-(acyl-carrier-protein) reductase, is reported at a resolution of 2.25 Å. Its fold is highly similar to those of the existing structures from some well characterized pathogens, such as Mycobacterium tuberculosis and Burkholderia pseudomallei, but differs significantly from the analogous mammalian structure. Hence, drugs known to target the enzymes of pathogenic bacteria may serve as potential leads against Rickettsia, which is responsible for spotted fever and typhus and is found throughout the world.

PubMed: 21904060
DOI: 10.1107/S1744309111030673

実験手法

X-RAY DIFFRACTION (2.25 Å)