2HMV

Diamond-shaped octameric ring structure of an RCK domain with ADP bound

Summary for 2HMV

• Entry DOI: 10.2210/pdb2hmv/pdb
• Related: 1LNQ 1LSS 1LSU 2HMS 2HMT 2HMU 2HMW
• Descriptor: YuaA protein, ADENOSINE-5'-DIPHOSPHATE (3 entities in total)
• Functional Keywords: rck, ktn, ktr, ktra, ktrab, membrane protein, ion transporter, symporter, transport protein
• Biological source: Bacillus subtilis
• Cellular location: Cell membrane ; Peripheral membrane protein ; Cytoplasmic side : O32080
• Total number of polymer chains: 2
• Total formula weight: 33007.30

Authors

Albright, R.A.,Morais-Cabral, J.H. (deposition date: 2006-07-11, release date: 2006-09-26, Last modification date: 2023-08-30)

Primary citation

Albright, R.A.,Ibar, J.L.,Kim, C.U.,Gruner, S.M.,Morais-Cabral, J.H.
The RCK Domain of the KtrAB K(+) Transporter: Multiple Conformations of an Octameric Ring.
Cell(Cambridge,Mass.), 126:1147-1159, 2006

PubMed Abstract: The KtrAB ion transporter is a complex of the KtrB membrane protein and KtrA, an RCK domain. RCK domains regulate eukaryotic and prokaryotic membrane proteins involved in K(+) transport. Conflicting functional models have proposed two different oligomeric arrangements for RCK domains, tetramer versus octamer. Our results for the KtrAB RCK domain clearly show an octamer in solution and in the crystal. We determined the structure of this protein in three different octameric ring conformations that resemble the RCK-domain octamer observed in the MthK potassium channel but show striking differences in size and symmetry. We present experimental evidence for the association between one RCK octameric ring and two KtrB membrane proteins. These results provide insights into the quaternary organization of the KtrAB transporter and its mechanism of activation and show that the RCK-domain octameric ring model is generally applicable to other ion-transport systems.

PubMed: 16990138
DOI: 10.1016/j.cell.2006.08.028

Experimental method

X-RAY DIFFRACTION (2.2 Å)