7l1e

The Crystal Structure of Bromide-Bound GtACR1

spinqualitylabelsall models 7l1e, resolution 3.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7l1e is a 2 chain structure with sequence from Guillardia theta. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.2Å Ligands: BR, GOL, LYR, OLC Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function L1J207_GUITC Publication Abstract from PubMed The crystal structure of the light-gated anion channel GtACR1 reported in our previous Research Article (Li et al., 2019) revealed a continuous tunnel traversing the protein from extracellular to intracellular pores. We proposed the tunnel as the conductance channel closed by three constrictions: C1 in the extracellular half, mid-membrane C2 containing the photoactive site, and C3 on the cytoplasmic side. Reported here, the crystal structure of bromide-bound GtACR1 reveals structural changes that relax the C1 and C3 constrictions, including a novel salt-bridge switch mechanism involving C1 and the photoactive site. These findings indicate that substrate binding induces a transition from an inactivated state to a pre-activated state in the dark that facilitates channel opening by reducing free energy in the tunnel constrictions. The results provide direct evidence that the tunnel is the closed form of the channel of GtACR1 and shed light on the light-gated channel activation mechanism. The crystal structure of bromide-bound GtACR1 reveals a pre-activated state in the transmembrane anion tunnel.,Li H, Huang CY, Govorunova EG, Sineshchekov OA, Yi A, Rothschild KJ, Wang M, Zheng L, Spudich JL Elife. 2021 May 17;10. pii: 65903. doi: 10.7554/eLife.65903. PMID:33998458 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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