Crystal structure of calcium dodecin (Rv0379), from Mycobacterium tuberculosis with a unique calcium-binding site. Academic Article

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.

authors

• Sacchettini, James

published proceedings

• Protein Sci

author list (cited authors)

• Arockiasamy, A., Aggarwal, A., Savva, C. G., Holzenburg, A., & Sacchettini, J. C.

citation count

• 7

complete list of authors

• Arockiasamy, Arulandu||Aggarwal, Anup||Savva, Christos G||Holzenburg, Andreas||Sacchettini, James C

publication date

• May 2011

publisher

• Wiley  Publisher

published in

• Protein Science  Journal

keywords

• Amino Acid Motifs
• Amino Acid Sequence
• Bacterial Proteins
• Binding Sites
• Calcium
• Calcium-Binding Proteins
• Crystallography, X-Ray
• Microscopy, Electron
• Models, Molecular
• Molecular Sequence Data
• Mycobacterium Tuberculosis
• Protein Binding
• Protein Structure, Tertiary
• Sequence Homology, Amino Acid
• Spectrophotometry, Atomic

PubMed Central ID

• 21370306

Digital Object Identifier (DOI)

• 10.1002/pro.607

start page

• 827

end page

• 833

volume

• 20

issue

• 5

URL

• http://dx.doi.org/10.1002/pro.607