Work

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

Year: 2013

Type: article

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.

Source: Protein Science

DOI: 10.1002/pro.2284

Authors: Pedro Serrano, Michael Geralt, Biswaranjan Mohanty, Kurt Wüthrich

Institutions: Joint Center for Structural Genomics, Scripps Research Institute

Language: English

Topic: Protein Structure and Dynamics

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: bronze

Funders: National Institutes of Health, National Institute of General Medical Sciences

Awards: Joint Center for Structural Genomics, Joint Center for Structural Genomics (JCSG-2)