3pjz

Crystal Structure of the Potassium Transporter TrkH from Vibrio parahaemolyticus

spinqualitylabelsall models 3pjz, resolution 3.51Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3pjz is a 2 chain structure with sequence from "oceanomonas_parahaemolytica"_(fujino_et_al._1951)_miyamoto_et_al._1961 "oceanomonas parahaemolytica" (fujino et al. 1951) miyamoto et al. 1961. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: K Gene: VP0032 ("Oceanomonas parahaemolytica" (Fujino et al. 1951) Miyamoto et al. 1961) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [TRKH_VIBPA] Low-affinity potassium transport system. Interacts with trk system potassium uptake protein TrkA and requires TrkE for transport activity. Selective for permeation of potassium ion and rubidium ion over smaller ions such as natrium or litium. Publication Abstract from PubMed The TrkH/TrkG/KtrB proteins mediate K(+) uptake in bacteria and probably evolved from simple K(+) channels by multiple gene duplications or fusions. Here we present the crystal structure of a TrkH from Vibrio parahaemolyticus. TrkH is a homodimer, and each protomer contains an ion permeation pathway. A selectivity filter, similar in architecture to those of K(+) channels but significantly shorter, is lined by backbone and side-chain oxygen atoms. Functional studies showed that TrkH is selective for permeation of K(+) and Rb(+) over smaller ions such as Na(+) or Li(+). Immediately intracellular to the selectivity filter are an intramembrane loop and an arginine residue, both highly conserved, which constrict the permeation pathway. Substituting the arginine with an alanine significantly increases the rate of K(+) flux. These results reveal the molecular basis of K(+) selectivity and suggest a novel gating mechanism for this large and important family of membrane transport proteins. Crystal structure of a potassium ion transporter, TrkH.,Cao Y, Jin X, Huang H, Derebe MG, Levin EJ, Kabaleeswaran V, Pan Y, Punta M, Love J, Weng J, Quick M, Ye S, Kloss B, Bruni R, Martinez-Hackert E, Hendrickson WA, Rost B, Javitch JA, Rajashankar KR, Jiang Y, Zhou M Nature. 2011 Feb 13. PMID:21317882 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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