Crystal structures of an Extracytoplasmic Solute Receptor from a TRAP transporter in its open and closed forms reveal a helix-swapped dimer requiring a cation for α-keto acid binding-5

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Taken from "Crystal structures of an Extracytoplasmic Solute Receptor from a TRAP transporter in its open and closed forms reveal a helix-swapped dimer requiring a cation for α-keto acid binding"

BMC Structural Biology 2007;7():11-11.

Published online 15 Mar 2007

PMCID:PMC1839085.

es involved in the binding of the ligand. The sodium ion is represented as a purple sphere. The helix in red, visible at bottom of the panel, belongs to the other monomer. : View of the overall changes induced by ligand binding. The unliganded protein is displayed as a cyan ribbon and the liganded protein is gray. For clarity, only the bound state of the other monomer is shown (gray surface). The distance between the two molecules of pyruvate from each monomer is 35Å. : View of the interdomain closing (C, no ligand; D, liganded protein). TakP is represented in CPK, with the same color coding as in A, except for the residues interacting with sodium pyruvate, which are pictured dark blue and orange for residues belonging to Domain I and II, respectively. The pyruvate molecule (black, barely visible) is completely buried.