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- Title
Crystal structure of a hypothetical protein from Giardia lamblia.
- 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.
- 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.
- Subjects
HAMPTON University (Va.); GIARDIA lamblia; PROTEIN structure; CRYSTAL structure; SMALL molecules; GIARDIASIS; COMMUNICABLE diseases
- Publication
Acta Crystallographica: Section F, Structural Biology Communications, 2022, Vol 78, Issue 2, p59
- ISSN
2053-230X
- Publication type
Article
- DOI
10.1107/S2053230X21013595