ArticleProtein science : a publication of the Protein Society2013
Structural representative of the protein family PF14466 has a new fold and establishes links with the C2 and PLAT domains from the widely distant Pfams PF00168 and PF01477.
Article in Protein science : a publication of the Protein Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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5 citing papers in PubMed.
- Protein salvage and repurposing in evolution: Phospholipase D toxins are stabilized by a remodeled scrap of a membrane association domain.Protein science : a publication of the Protein Society · 2023Article
- Identification of nuclear genes controlling chlorophyll synthesis in barley by RNA-seq.BMC plant biology · 2016Article
- NMR reveals structural rearrangements associated to substrate insertion in nucleotide-adding enzymes.Protein science : a publication of the Protein Society · 2016Article
- Three DUF1996 Proteins Localize in Vacuoles and Function in Fungal Responses to Multiple Stresses and Metal Ions.Scientific reports · 2016Article
- NMR-profiles of protein solutions.Biopolymers · 2013Article
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Abstract
The domain of unknown function (DUF) YP_001302112.1, a protein secreted by the human intestinal microbita, has been determined by NMR and represents the first structure for the Pfam PF14466. Its NMR structure is classified as a new fold, which, nonetheless, shows limited similarities with representatives of the PLAT/LH2 domains from PF01477 and the C2 domains from PF00168, both of which bind Ca(2+) for their physiological functions. Further experiments revealed affinity of YP_001302112.1 for Ca(2+), and the NMR structure in the presence of CaCl2 was better defined than that of the apo-protein. Overall, these NMR structures establish a new connection between structural representatives from two widely different Pfams that include the calcium-binding domain of a sialidase from Vibrio cholerae and the α-toxin from Clostridium perfrigens, whereby these two proteins have only 7% sequence identity. Furthermore, it provides information toward the functional annotation of YP_001302112.1, based on its capacity to bind Ca(2+), and thus adds to the structural and functional coverage of the protein sequence universe.
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