1UL3

Crystal Structure of PII from Synechocystis sp. PCC 6803

1UL3 の概要

• エントリーDOI: 10.2210/pdb1ul3/pdb
• 関連するPDBエントリー: 1hwu 2pii
• 分子名称: Nitrogen regulatory protein P-II, GLYCEROL, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: nitrogen regulation, cyanobacteria, signaling protein
• 由来する生物種: Synechocystis sp.
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 49925.84

構造登録者

Xu, Y.,Carr, P.D.,Clancy, P.,Garcia-Dominguez, M.,Forchhammer, K.,Florencio, F.,Tandeau de Marsac, N.,Vasudevan, S.G.,Ollis, D.L. (登録日: 2003-09-09, 公開日: 2003-12-16, 最終更新日: 2023-10-25)

主引用文献

Xu, Y.,Carr, P.D.,Clancy, P.,Garcia-Dominguez, M.,Forchhammer, K.,Florencio, F.,Vasudevan, S.G.,Tandeau de Marsac, N.,Ollis, D.L.
The structures of the PII proteins from the cyanobacteria Synechococcus sp. PCC 7942 and Synechocystis sp. PCC 6803.
Acta Crystallogr.,Sect.D, 59:2183-2190, 2003

PubMed Abstract: The PII proteins from the cyanobacteria Synechococcus sp. PCC 7942 and Synechocystis sp. PCC 6803 have been crystallized and high-resolution structures have been obtained using X-ray crystallography. The core of these new structures is similar to that of the PII proteins from Escherichia coli, although the structures of the T- and C-loops differ. The T-loop of the Synechococcus protein is ordered, but appears to be stabilized by crystal contacts. The same loop in the Synechocystis protein is disordered. The C-terminus of the Synechocystis protein is stabilized by hydrogen bonding to the same region of a crystallographically related molecule. The same terminus in the Synechococcus protein is stabilized by coordination with a metal ion. These observations are consistent with the idea that both the T-loop and the C-terminus of PII proteins are flexible in solution and that this flexibility may be important for receptor recognition. Sequence comparisons are used to identify regions of the sequence unique to the cyanobacteria.

PubMed: 14646076
DOI: 10.1107/S0907444903019589

実験手法

X-RAY DIFFRACTION (2 Å)