Loading
PDBj
メニューPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

3NPH

Crystal structure of the pfam00427 domain from Synechocystis sp. PCC 6803

3NPH の概要
エントリーDOI10.2210/pdb3nph/pdb
分子名称Phycobilisome 32.1 kDa linker polypeptide, phycocyanin-associated, rod 2 (2 entities in total)
機能のキーワードpfam00427 domain, linker protein, phycobiliprotein, photosynthesis
由来する生物種Synechocystis sp.
細胞内の位置Cellular thylakoid membrane; Peripheral membrane protein; Cytoplasmic side (By similarity): P73204
タンパク質・核酸の鎖数1
化学式量合計17458.37
構造登録者
Gao, X.,Chen, L.,Wu, J.-W.,Zhang, Y.-Z. (登録日: 2010-06-28, 公開日: 2011-06-29, 最終更新日: 2023-12-27)
主引用文献Gao, X.,Zhang, N.,Wei, T.-D.,Su, H.-N.,Xie, B.-B.,Dong, C.-C.,Zhang, X.-Y.,Chen, X.-L.,Zhou, B.-C.,Wang, Z.-X.,Wu, J.-W.,Zhang, Y.-Z.
Crystal structure of the N-terminal domain of linker L(R) and the assembly of cyanobacterial phycobilisome rods
Mol.Microbiol., 82:698-705, 2011
Cited by
PubMed Abstract: Phycobilisomes are light-harvesting supramolecular complexes in cyanobacteria and red algae. Linkers play a pivotal role in the assembly and energy transfer modulation of phycobilisomes. However, how linkers function remains unclear due to the lack of structural and biochemical studies of linkers, especially the N-terminal domain of L(R) (pfam00427). Here, we report the crystal structure of the pfam00427 domain of the linker L(R) (30) from Synechocystis sp. PCC 6803 at 1.9 Å. The pfam00427 presents as a previously uncharacterized point symmetric six α-helix bundle. To elucidate the binding style of pfam00427 in the C-phycocyanin (C-PC) (αβ)(6) hexamer, we fixed pfam00427 computationally into the C-PC (αβ)(6) inner cavity using the program AutoDock. Combined with a conserved 'C-PC binding patch' on pfam00427 identified, we arrived at a model for the pfam00427-C-PC (αβ)(6) complex. This model was further optimized and evaluated as a reasonable result by a molecular dynamics simulation. In the resulting model, the pfam00427 domain is stably positioned in the central hole of the C-PC trimer. Moreover, the L(RT) (pfam01383) was docked into our pfam00427-C-PC model to generate a complete phycobilisome rod in which the linkers join individual biliprotein hexamers.
PubMed: 21923764
DOI: 10.1111/j.1365-2958.2011.07844.x
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.849 Å)
構造検証レポート
Validation report summary of 3nph
検証レポート(詳細版)ダウンロードをダウンロード

248335

件を2026-01-28に公開中

PDB statisticsPDBj update infoContact PDBjnumon