Structural highlights
Publication Abstract from PubMed
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 identify the orthologs of Ca dodecins with different ligand-binding specificity.
Crystal structure of the calcium chelating immunodominant antigen, calcium dodecin (Rv0379), from Mycobacterium tuberculosis with a unique calcium-binding site.,Arockiasamy A, Aggarwal A, Savva CG, Holzenburg A, Sacchettini JC Protein Sci. 2011 Mar 2. doi: 10.1002/pro.607. PMID:21370306[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Arockiasamy A, Aggarwal A, Savva CG, Holzenburg A, Sacchettini JC. Crystal structure of the calcium chelating immunodominant antigen, calcium dodecin (Rv0379), from Mycobacterium tuberculosis with a unique calcium-binding site. Protein Sci. 2011 Mar 2. doi: 10.1002/pro.607. PMID:21370306 doi:10.1002/pro.607
