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3F9I

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

Summary for 3F9I
Entry DOI10.2210/pdb3f9i/pdb
Descriptor3-oxoacyl-[acyl-carrier-protein] reductase (2 entities in total)
Functional Keywords3-ketoacyl-(acyl-carrier-protein) reductase, rickettsia, fatty acid biosynthesis, lipid synthesis, nadp, oxidoreductase, structural genomics, seattle structural genomics center for infectious disease, ssgcid
Biological sourceRickettsia prowazekii
Total number of polymer chains2
Total formula weight53637.98
Authors
Seattle Structural Genomics Center for Infectious Disease (SSGCID) (deposition date: 2008-11-13, release date: 2008-11-25, Last modification date: 2023-09-06)
Primary citationSubramanian, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.25 Å)
Structure validation

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数据于2024-11-06公开中

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