Crystal structure of calcium dodecin (Rv0379), from Mycobacterium tuberculosis with a unique calcium-binding site |
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Authors: | Arockiasamy Arulandu Aggarwal Anup Savva Christos G Holzenburg Andreas Sacchettini James C |
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Affiliation: | 1Department of Biochemistry and Biophysics, Texas A&M University, College Station, Texas 77843-2128;2Microscopy and Imaging Center and Department of Biology, Texas A&M University, Biological Sciences Building West, College Station, Texas 77843-2257;3Center for Structural Biology, Institute of Biosciences and Technology, Houston, Texas 77030 |
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Abstract: | In eukaryotes, calcium-binding proteins play a pivotal role in diverse cellular processes, and recent findings suggest similar roles for bacterial proteins at different stages in their life cycle. Here, we report the crystal structure of calcium dodecin, Rv0379, from Mycobacterium tuberculosis with a dodecameric oligomeric assembly and a unique calcium-binding motif. Structure and sequence analysis were used to identify orthologs of Rv0379 with different ligand-binding specificity. |
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Keywords: | calcium‐binding dodecin Mycobacterium tuberculosis dodecamer bidentate binding distorted hexagonal bipyramid |
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