1E29

PSII associated cytochrome C549 from Synechocystis sp.

1E29 の概要

• エントリーDOI: 10.2210/pdb1e29/pdb
• 分子名称: CYTOCHROME C549, HEME C, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: electron transport, psii associated cytochrome, cytochrome, low potential, bis_histidinyl, psii modulator
• 由来する生物種: SYNECHOCYSTIS SP
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15873.44

構造登録者

Frazao, C.,Enguita, F.J.,Coelho, R.,Sheldrick, G.M. (登録日: 2000-05-19, 公開日: 2001-05-04, 最終更新日: 2024-11-06)

主引用文献

Frazao, C.,Enguita, F.J.,Coelho, R.,Sheldrick, G.M.,Navarro, J.A.,Hervas, M.,De La Rosa, M.A.,Carrondo, M.A.
Crystal Structure of Low-Potential Cytochrome C549 from Synechocystis Sp. Pcc 6803 at 1.21A Resolution
J.Biol.Inorg.Chem., 6:324-, 2001

PubMed Abstract: The crystal structure of low-potential cytochrome c549, an extrinsic component of the photosystem II (PS II) from Synechocystis sp. PCC 6803, was obtained directly from single-wavelength 1.21 A resolution diffraction data. This is the first monodomain bis-histidinyl monoheme cytochrome c to be structurally characterized. The extended N-terminal region of c549 builds up a two-strand antiparallel beta-sheet in a hairpin motif, which extends through two molecules owing to crystal packing. Both peptide termini are involved in crystal contacts, which may explain their protrusion out of the globular fold. The C-terminus is preceded by a 9 A-long hydrophobic finger extending from a positively charged base and could be involved in PSII interactions, as well as a protruding negative patch built by a set of conserved acidic residues among c549 sequences.

PubMed: 11315568
DOI: 10.1007/S007750100208

実験手法

X-RAY DIFFRACTION (1.21 Å)