1HWU

STRUCTURE OF PII PROTEIN FROM HERBASPIRILLUM SEROPEDICAE

1HWU の概要

• エントリーDOI: 10.2210/pdb1hwu/pdb
• 関連するPDBエントリー: 2PII
• 分子名称: PII PROTEIN (2 entities in total)
• 機能のキーワード: herbaspirillum seropedicae pii, beta-alpha-beta motif, signal transduction protein, signaling protein
• 由来する生物種: Herbaspirillum seropedicae
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 73705.13

構造登録者

Benelli, E.M.,Buck, M.,Polikarpov, I.,De Souza, E.M.,Cruz, L.M.,Pedrosa, F.O. (登録日: 2001-01-10, 公開日: 2003-06-17, 最終更新日: 2023-08-09)

主引用文献

Machado Benelli, E.,Buck, M.,Polikarpov, I.,Maltempi de Souza, E.,Cruz, L.M.,Pedrosa, F.O.
Herbaspirillum seropedicae signal transduction protein PII is structurally similar to the enteric GlnK.
Eur.J.Biochem., 269:3296-3303, 2002

PubMed Abstract: PII-like proteins are signal transduction proteins found in bacteria, archaea and eukaryotes. They mediate a variety of cellular responses. A second PII-like protein, called GlnK, has been found in several organisms. In the diazotroph Herbaspirillum seropedicae, PII protein is involved in sensing nitrogen levels and controlling nitrogen fixation genes. In this work, the crystal structure of the unliganded H. seropedicae PII was solved by X-ray diffraction. H. seropedicae PII has a Gly residue, Gly108 preceding Pro109 and the main-chain forms a beta turn. The glycine at position 108 allows a bend in the C-terminal main-chain, thereby modifying the surface of the cleft between monomers and potentially changing function. The structure suggests that the C-terminal region of PII proteins may be involved in specificity of function, and nonenteric diazotrophs are found to have the C-terminal consensus XGXDAX(107-112). We are also proposing binding sites for ATP and 2-oxoglutarate based on the structural alignment of PII with PII-ATP/GlnK-ATP, 5-carboxymethyl-2-hydroxymuconate isomerase and 4-oxalocrotonate tautomerase bound to the inhibitor 2-oxo-3-pentynoate.

PubMed: 12084071
DOI: 10.1046/j.1432-1033.2002.03011.x

実験手法

X-RAY DIFFRACTION (2.1 Å)