title: New protein fold revealed by a 1.65 A resolution crystal structure of Francisella tularensis pathogenicity island protein IglC.
abstract: Francisella tularensis is a highly infectious Gram-negative intracellular pathogen that causes the fulminating disease tularemia and is considered to be a potential bioweapon. F. tularensis pathogenicity island proteins play a key role in modulating phagosome biogenesis and subsequent bacterial escape into the cytoplasm of macrophages. The 23 kDa pathogenicity island protein IglC is essential for the survival and proliferation of F. tularensis in macrophages. Seeking to gain some insight into its function, we determined the crystal structure of IglC at 1.65 A resolution. IglC adopts a beta-sandwich conformation that exhibits no similarity with any known protein structure.
authors: Macromolecular Crystallography Laboratory, Center for Cancer Research, National Cancer Institute at Frederick, MD 21702-1201, USA.
authors: Ping
authors: P
authors: Sun
authors: Brian P
authors: BP
authors: Austin
authors: Florian D
authors: FD
authors: Schubot
authors: David S
authors: DS
authors: Waugh
mesh_terms: D001426:Bacterial Proteins; D019295:Computational Biology / Q000379:methods*; D018360:Crystallography, X-Ray / Q000379:methods*; D005604:Francisella tularensis / Q000378:metabolism*; D044404:Genomic Islands; D008958:Models, Molecular; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D040901:Proteomics / Q000379:methods; D037521:Virulence Factors / Q000737:chemistry
chemical_list: D001426:Bacterial Proteins; D037521:Virulence Factors