3AKA

Structural basis for prokaryotic calcium-mediated regulation by a Streptomyces coelicolor calcium-binding protein

Summary for 3AKA

• Entry DOI: 10.2210/pdb3aka/pdb
• Related: 3AKB
• Descriptor: Putative calcium binding protein, CALCIUM ION (3 entities in total)
• Functional Keywords: calcium-binding protein, ef-hand, metal binding protein
• Biological source: Streptomyces coelicolor
• Total number of polymer chains: 1
• Total formula weight: 18027.14

Authors

Zhao, X.,Pang, H.,Wang, S.,Zhou, W.,Yang, K.,Bartlam, M. (deposition date: 2010-07-09, release date: 2011-01-26, Last modification date: 2024-04-03)

Primary citation

Zhao, X.,Pang, H.,Wang, S.,Zhou, W.,Yang, K.,Bartlam, M.
Structural basis for prokaryotic calciummediated regulation by a Streptomyces coelicolor calcium binding protein
Protein Cell, 1:771-779, 2010

PubMed Abstract: The important and diverse regulatory roles of Ca(2+) in eukaryotes are conveyed by the EF-hand containing calmodulin superfamily. However, the calcium-regulatory proteins in prokaryotes are still poorly understood. In this study, we report the three-dimensional structure of the calcium-binding protein from Streptomyces coelicolor, named CabD, which shares low sequence homology with other known helix-loop-helix EF-hand proteins. The CabD structure should provide insights into the biological role of the prokaryotic calcium-binding proteins. The unusual structural features of CabD compared with prokaryotic EF-hand proteins and eukaryotic sarcoplasmic calcium-binding proteins, including the bending conformation of the first C-terminal α-helix, unpaired ligand-binding EF-hands and the lack of the extreme C-terminal loop region, suggest it may have a distinct and significant function in calcium-mediated bacterial physiological processes, and provide a structural basis for potential calcium-mediated regulatory roles in prokaryotes.

PubMed: 21203918
DOI: 10.1007/s13238-010-0085-z

Experimental method

X-RAY DIFFRACTION (1.8 Å)