3IIU

Structure of the reconstituted Peridinin-Chlorophyll a-Protein (RFPCP) mutant N89L

3IIU の概要

• エントリーDOI: 10.2210/pdb3iiu/pdb
• 関連するPDBエントリー: 1PPR 2C9E 3IIS
• 分子名称: Peridinin-chlorophyll a-binding protein 1, chloroplastic, CHLOROPHYLL A, PERIDININ, ... (7 entities in total)
• 機能のキーワード: alpha helical, light harvesting protein, photosynthesis, carotenoids, dinoflagellates, chlorophyll, chloroplast, chromophore, light-harvesting polypeptide, transit peptide
• 由来する生物種: Amphidinium carterae (Dinoflagellate)
• 細胞内の位置: Plastid, chloroplast: P80484
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 21031.05

構造登録者

Schulte, T.,Hofmann, E. (登録日: 2009-08-03, 公開日: 2009-11-24, 最終更新日: 2023-09-06)

主引用文献

Schulte, T.,Niedzwiedzki, D.M.,Birge, R.R.,Hiller, R.G.,Polivka, T.,Hofmann, E.,Frank, H.A.
Identification of a single peridinin sensing Chl-a excitation in reconstituted PCP by crystallography and spectroscopy.
Proc.Natl.Acad.Sci.USA, 106:20764-20769, 2009

PubMed Abstract: The peridinin-chlorophyll a-protein (PCP) of dinoflagellates is unique among the large variety of natural photosynthetic light-harvesting systems. In contrast to other chlorophyll protein complexes, the soluble PCP is located in the thylakoid lumen, and the carotenoid pigments outnumber the chlorophylls. The structure of the PCP complex consists of two symmetric domains, each with a central chlorophyll a (Chl-a) surrounded by four peridinin molecules. The protein provides distinctive surroundings for the pigment molecules, and in PCP, the specific environment around each peridinin results in overlapping spectral line shapes, suggestive of different functions within the protein. One particular Per, Per-614, is hypothesized to show the strongest electronic interaction with the central Chl-a. We have performed an in vitro reconstitution of pigments into recombinant PCP apo-protein (RFPCP) and into a mutated protein with an altered environment near Per-614. Steady-state and transient optical spectroscopic experiments comparing the RFPCP complex with the reconstituted mutant protein identify specific amino acid-induced spectral shifts. The spectroscopic assignments are reinforced by a determination of the structures of both RFPCP and the mutant by x-ray crystallography to a resolution better than 1.5 A. RFPCP and mutated RFPCP are unique in representing crystal structures of in vitro reconstituted light-harvesting pigment-protein complexes.

PubMed: 19934052
DOI: 10.1073/pnas.0908938106

実験手法

X-RAY DIFFRACTION (1.45 Å)