Biomaterial Database

The complete amino acid sequences of the B800-850 antenna polypeptides from Rhodopseudomonas acidophila strain 7750. 1988

I Bissig, and R A Brunisholz, and F Suter, and R J Cogdell, and H Zuber

Institut für Molekularbiologie und Biophysik, ETH-Hönggerberg, Zürich.

Spectrally pure B800-850 light harvesting complexes of Rhodopseudomonas acidophila 7750 were prepared by chromatography of LDAO-solubilised photosynthetic membranes on Whatmann DE-52 ion exchange resin. Two low molecular mass polypeptides (alpha, beta) have been isolated by organic solvent extraction of the lyophilised B800-850 light harvesting complexes. Their primary structures were determined by liquid phase sequencer runs, by the sequence analyses of C-terminal o-iodosobenzoic acid fragments, by hydrazinolysis and by carboxypeptidase degradation. B800-850 alpha consists of 53 amino acids and is 45.3% and 50.9% homologous to the B800-850-alpha antenna polypeptides of Rhodobacter sphaeroides and Rhodobacter capsulatus, respectively. The second very short polypeptide (B800-850-beta, 41 amino acids) is 61.0% and 56.1% homologous to the corresponding polypeptides of Rb. sphaeroides and Rb. capsulatus. The molar ratio of the two polypeptides is about 1:1. Both polypeptides show a hydrophilic N-terminal domain, a very hydrophobic central domain and a short C-terminal domain. In both polypeptides the typical His residues, identified in all antenna polypeptides of purple nonsulphur bacteria as possible bacteriochlorophyll binding sites, were found.

UI	MeSH Term	Description	Entries
D008969	Molecular Sequence Data	Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.	Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D010860	Pigments, Biological	Any normal or abnormal coloring matter in PLANTS; ANIMALS or micro-organisms.	Biological Pigments
D000595	Amino Acid Sequence	The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.	Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D001426	Bacterial Proteins	Proteins found in any species of bacterium.	Bacterial Gene Products,Bacterial Gene Proteins,Gene Products, Bacterial,Bacterial Gene Product,Bacterial Gene Protein,Bacterial Protein,Gene Product, Bacterial,Gene Protein, Bacterial,Gene Proteins, Bacterial,Protein, Bacterial,Proteins, Bacterial
D012241	Rhodopseudomonas	A genus of gram-negative, rod-shaped, phototrophic bacteria found in aquatic environments. Internal photosynthetic membranes are present as lamellae underlying the cytoplasmic membrane.
D013045	Species Specificity	The restriction of a characteristic behavior, anatomical structure or physical system, such as immune response; metabolic response, or gene or gene variant to the members of one species. It refers to that property which differentiates one species from another but it is also used for phylogenetic levels higher or lower than the species.	Species Specificities,Specificities, Species,Specificity, Species
D045332	Photosystem II Protein Complex	A large multisubunit protein complex found in the THYLAKOID MEMBRANE. It uses light energy derived from LIGHT-HARVESTING PROTEIN COMPLEXES to catalyze the splitting of WATER into DIOXYGEN and of reducing equivalents of HYDROGEN.	Chloroplast Reaction Center Protein D1,D1 Photosystem II Protein, Plant,Light-Induced D1 Protein, Photosystem II,Oxygen Evolving Enzyme,PRCP II D2 Protein,Photosystem II,Photosystem II Reaction Center,Photosystem II Reaction Center Complex D1 Protein,Photosystem II Reaction Center Complex D2 Protein,RCII-D1 Protein,Water Oxidase,Water-Splitting Enzyme of Photosynthesis,Enzyme, Oxygen Evolving,Evolving Enzyme, Oxygen,Light Induced D1 Protein, Photosystem II,Oxidase, Water,Photosynthesis Water-Splitting Enzyme,Water Splitting Enzyme of Photosynthesis
D045342	Light-Harvesting Protein Complexes	Complexes containing CHLOROPHYLL and other photosensitive molecules. They serve to capture energy in the form of PHOTONS and are generally found as components of the PHOTOSYSTEM I PROTEIN COMPLEX or the PHOTOSYSTEM II PROTEIN COMPLEX.	Antenna Complexes, Light-Harvesting,Light-Harvesting Antenna Complexes,Light-Harvesting Chlorophyll Protein,Light-Harvesting Chlorophyll Protein Complexes,Antenna Complexes, Light Harvesting,Chlorophyll Protein, Light-Harvesting,Complexes, Light-Harvesting Antenna,Complexes, Light-Harvesting Protein,Light Harvesting Antenna Complexes,Light Harvesting Chlorophyll Protein,Light Harvesting Chlorophyll Protein Complexes,Light Harvesting Protein Complexes,Protein Complexes, Light-Harvesting