5uk6

Structure of Anabaena Sensory Rhodopsin Determined by Solid State NMR Spectroscopy and DEER

spinqualitylabelsall models 5uk6 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5uk6 is a 3 chain structure with sequence from Nostoc sp. PCC 7120 = FACHB-418. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solid-state NMR, 10 models Ligands: LYR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q8YSC4_NOSS1 Publication Abstract from PubMed Oligomerization of membrane proteins is common in nature. Here, we combine spin-labeling double electron-electron resonance (DEER) and solid-state NMR (ssNMR) spectroscopy to refine the structure of an oligomeric integral membrane protein, Anabaena sensory rhodopsin (ASR), reconstituted in a lipid environment. An essential feature of such a combined approach is that it provides structural distance restraints spanning a range of ca 3-60A while using the same sample preparation (i.e., mutations, paramagnetic labeling, and reconstitution in lipid bilayers) for both ssNMR and DEER. Direct modeling of the multispin effects on DEER signal allowed for the determination of the oligomeric order and for obtaining long-range DEER distance restraints between the ASR trimer subunits that were used to refine the ssNMR structure of ASR. The improved structure of the ASR trimer revealed a more compact packing of helices and side chains at the intermonomer interface, compared to the structure determined using the ssNMR data alone. The extent of the refinement is significant when compared with typical helix movements observed for the active states of homologous proteins. Our combined approach of using complementary DEER and NMR measurements for the determination of oligomeric structures would be widely applicable to membrane proteins where paramagnetic tags can be introduced. Such a method could be used to study the effects of the lipid membrane composition on protein oligomerization and to observe structural changes in protein oligomers upon drug, substrate, and co-factor binding. Oligomeric Structure of Anabaena Sensory Rhodopsin in a Lipid Bilayer Environment by Combining Solid-State NMR and Long-range DEER Constraints.,Milikisiyants S, Wang S, Munro RA, Donohue M, Ward ME, Bolton D, Brown LS, Smirnova TI, Ladizhansky V, Smirnov AI J Mol Biol. 2017 Jun 16;429(12):1903-1920. doi: 10.1016/j.jmb.2017.05.005. Epub, 2017 May 10. PMID:28501588 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Bacteriorhodopsin 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA