4I0U

Improved structure of Thermotoga maritima CorA at 2.7 A resolution

Summary for 4I0U

• Entry DOI: 10.2210/pdb4i0u/pdb
• Descriptor: Magnesium transport protein CorA, MAGNESIUM ION, CHLORIDE ION, ... (7 entities in total)
• Functional Keywords: magnesium/cobalt transport, metal transport, membrane protein, cora
• Biological source: Thermotoga maritima
• Cellular location: Cell inner membrane; Multi-pass membrane protein: Q9WZ31
• Total number of polymer chains: 10
• Total formula weight: 419905.54

Authors

Nordin, N.,Guskov, A.,Phua, T.,Sahaf, N.,Xia, Y.,Lu, S.Y.,Eshaghi, H.,Eshaghi, S. (deposition date: 2012-11-19, release date: 2013-03-06, Last modification date: 2024-03-20)

Primary citation

Nordin, N.,Guskov, A.,Phua, T.,Sahaf, N.,Xia, Y.,Lu, S.Y.,Eshaghi, H.,Eshaghi, S.
Exploring the structure and function of Thermotoga maritima CorA reveals the mechanism of gating and ion selectivity in Co2+/Mg2+ transport.
Biochem.J., 451:365-374, 2013

PubMed Abstract: The CorA family of divalent cation transporters utilizes Mg2+ and Co2+ as primary substrates. The molecular mechanism of its function, including ion selectivity and gating, has not been fully characterized. Recently we reported a new structure of a CorA homologue from Methanocaldococcus jannaschii, which provided novel structural details that offered the conception of a unique gating mechanism involving conversion of an open hydrophilic gate into a closed hydrophobic one. In the present study we report functional evidence for this novel gating mechanism in the Thermotoga maritima CorA together with an improved crystal structure of this CorA to 2.7 Å (1 Å=0.1 nm) resolution. The latter reveals the organization of the selectivity filter to be similar to that of M. jannaschii CorA and also the previously unknown organization of the second signature motif of the CorA family. The proposed gating is achieved by a helical rotation upon the binding of a metal ion substrate to the regulatory binding sites. Additionally, our data suggest that the preference of this CorA for Co2+ over Mg2+ is controlled by the presence of threonine side chains in the channel. Finally, the roles of the intracellular metal-binding sites have been assigned to increased thermostability and regulation of the gating. These mechanisms most likely apply to the entire CorA family as they are regulated by the highly conserved amino acids.

PubMed: 23425532
DOI: 10.1042/BJ20121745

Experimental method

X-RAY DIFFRACTION (2.7 Å)