| Autor: |
Theiler R, Suter F, Pennoyer JD, Zuber H, Niederman RA |
| Jazyk: |
angličtina |
| Zdroj: |
FEBS letters [FEBS Lett] 1985 May 20; Vol. 184 (2), pp. 231-6. |
| DOI: |
10.1016/0014-5793(85)80612-8 |
| Abstrakt: |
The complete amino acid sequence was determined for the alpha- and beta-chains of the B875 light-harvesting protein purified from photosynthetic membranes of Rhodopseudomonas sphaeroides 2.4.1. The sequence of the B875-alpha-polypeptide was identical to that reported for the R26.1 carotenoidless mutant [(1985) Biochim. Biophys. Acta 806, 185-186] and contained 58 amino acid residues with a blocked methionine and a glutamic acid at the N- and C-termini, respectively. The B875-beta-polypeptide contained 48 amino acid residues with alanine and phenylalanine as respective N- and C-termini; although otherwise identical, the leucine at position 29 in the wild-type strain was replaced by proline in the mutant. This radical amino acid substitution occurred within the central hydrophobic domain of the beta-polypeptide chain and is thought to result in a weakening of the structure of the alpha/beta heterodimer since it was not possible to isolate the intact pigment-protein complex from the R26.1 mutant strain. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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