2hmw | pdb_00002hmw

Square-shaped octameric ring structure of an RCK domain with ATP bound

spinqualitylabelsall models 2hmw, resolution 3.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2hmw is a 2 chain structure with sequence from "bacillus_globigii"_migula_1900 "bacillus globigii" migula 1900. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ATP Related: 1lsu, 1lss, 1lnq, 2hmt, 2hmu, 2hmv, 2hms Gene: yuaA ("Bacillus globigii" Migula 1900) Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. The RCK domain of the KtrAB K+ transporter: multiple conformations of an octameric ring.,Albright RA, Ibar JL, Kim CU, Gruner SM, Morais-Cabral JH Cell. 2006 Sep 22;126(6):1147-59. PMID:16990138 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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