title: Nuclear magnetic resonance secondary shifts of a light-harvesting 2 complex reveal local backbone perturbations induced by its higher-order interactions.
abstract: Protein nuclear magnetic resonance (NMR) secondary chemical shifts are widely used to predict the secondary structure, and in solid-state NMR, they are often the only unambiguous structural parameters available. However, the employed prediction methods are empirical in nature, relying on the assumption that secondary shifts are only affected by shielding effects of neighboring atoms. We analyzed the secondary shifts of a photosynthetic membrane protein with a high density of chromophores and very tight packing, the light-harvesting 2 (LH2) complex of Rhodopseudomonas acidophila. A relation was found between secondary shift anomalies and protein-protein or pigment-protein tertiary and quaternary contacts. For several residues, including the bacteriochlorophyll-coordinating histidines (alphaH31 and betaH30) and the phenylalanine alphaF41 that has strongly twisted C(b)-C(a)-C and C(a)-C-N conformations in the LH2 crystal structure, the perturbing effects on the backbone chemical shifts were tested by density functional theory (DFT) calculations. We propose that higher-order interactions in the tightly packed complex can induce localized perturbations of the backbone conformation and electronic structure, related to functional pigment-protein or protein-protein interactions.
authors: Leiden Institute of Chemistry, Leiden University, P.O. Box 9502, 2300 RA Leiden, The Netherlands. a.pandit@chem.leidenuniv.nl
authors: Anjali
authors: A
authors: Pandit
authors: Piotr K
authors: PK
authors: Wawrzyniak
authors: Adriaan J
authors: AJ
authors: van Gammeren
authors: Francesco
authors: F
authors: Buda
authors: Swapna
authors: S
authors: Ganapathy
authors: Huub J M
authors: HJ
authors: de Groot
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D002942:Circular Dichroism; D006639:Histidine / Q000235:genetics / Q000378:metabolism; D045342:Light-Harvesting Protein Complexes / Q000737:chemistry* / Q000378:metabolism; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation; D017510:Protein Folding; D012241:Rhodopseudomonas / Q000378:metabolism
chemical_list: D001426:Bacterial Proteins; D045342:Light-Harvesting Protein Complexes; D008565:Membrane Proteins; D006639:Histidine