Crystal structure of a hypothetical protein from Giardia lamblia. Issue 2 (28th January 2022)

• Record Type: Journal Article
• Authors: Beard, Dylan K.; Bristol, Seonna; Cosby, Kayla; Davis, Amber; Manning, Courtney; Perry, Lionel; Snapp, Lauren; Toy, Arian; Wheeler, Kayla; Young, Jeremy; Staker, Bart; Arakaki, Tracy L.; Abendroth, Jan; Subrahamanian, Sandhya; Edwards, Thomas E.; Myler, Peter J.; Asojo, Oluwatoyin A.
• Is Part Of: Acta crystallographica. Volume 78:Issue 2(2022)
• Page Start: 59
• Page End: 65
• Publication Date: 2022-01-28
• Subjects: giardiasis -- SSGCID -- infectious diseases -- travelers' diarrhea -- undergraduate education and training -- structural genomics; Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S2053230X21013595
• Languages: English
• ISSNs: 2053-230X

Abstract

Abstract : The 1.35 Å resolution crystal structure of a 15.6 kDa hypothetical protein from the parasite Giardia lamblia was determined as part of structural genomic studies to assign possible functions to hypothetical proteins from infectious agents. The structure has a prototypical endoribonuclease L‐PSP (liver perchloric acid‐soluble protein) topology with conserved allosteric active‐site residues despite lacking any appreciable sequence identity to other members of this superfamily. Abstract : Giardiasis is the most prevalent diarrheal disease globally and affects humans and animals. It is a significant problem in developing countries, the number one cause of travelers' diarrhea and affects children and immunocompromised individuals, especially HIV‐infected individuals. Giardiasis is treated with antibiotics (tinidazole and metronidazole) that are also used for other infections such as trichomoniasis. The ongoing search for new therapeutics for giardiasis includes characterizing the structure and function of proteins from the causative protozoan Giardia lamblia . These proteins include hypothetical proteins that share 30% sequence identity or less with proteins of known structure. Here, the atomic resolution structure of a 15.6 kDa protein was determined by molecular replacement. The structure has the two‐layer αβ‐sandwich topology observed in the prototypical endoribonucleases L‐PSPs (liver perchloric acid‐soluble proteins) with conserved allosteric active sites containing small molecules from the crystallization solution. This article is an educational collaboration between Hampton University and the Seattle Structural Genomics Center for Infectious Disease.