2PII

PII, GLNB PRODUCT

2PII の概要

• エントリーDOI: 10.2210/pdb2pii/pdb
• 分子名称: PII (2 entities in total)
• 機能のキーワード: signal transduction protein
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12443.44

構造登録者

Carr, P.D.,Cheah, E.,Suffolk, P.M.,Ollis, D.L. (登録日: 1995-05-02, 公開日: 1996-06-20, 最終更新日: 2024-02-21)

主引用文献

Carr, P.D.,Cheah, E.,Suffolk, P.M.,Vasudevan, S.G.,Dixon, N.E.,Ollis, D.L.
X-ray structure of the signal transduction protein from Escherichia coli at 1.9 A.
Acta Crystallogr.,Sect.D, 52:93-104, 1996

PubMed Abstract: The structure of the bacterial signal transduction protein P(II) has been refined to an R factor of 13.2% using 3sigma data between 10 and 1.9 A. The crystals exhibited twinning by merohedry and X-ray intensities were corrected using the method of Fisher & Sweet [Fisher & Sweet (1980). Acta Cryst. A36, 755-760] prior to refinement. Our earlier 2.7 A structure [Cheah, Carr, Suffolk, Vasudevan, Dixon & Ollis (1994). Structure, 2, 981-990] served as a starting model. P(II) is a trimeric molecule, each subunit has a mass of 12.4 kDa and contains 112 amino-acid residues. The refined model includes all 1065 protein atoms per subunit plus 312 water molecules. The high-resolution refinement confirms the correctness of our 2.7 A model, although it leads to a redefinition of the extent of various secondary-structural elements. The monomeric structure of P(II) exhibits an interlocking double betaalphabeta fold. This is a stable fold found in a number of proteins with diverse functions. The association of the protein into a trimer leads to a new structure which we describe in detail. The effects of crystal packing forces are discussed and potential interaction sites with other proteins and effector molecules are identified.

PubMed: 15299730
DOI: 10.1107/S0907444995007293

実験手法

X-RAY DIFFRACTION (1.9 Å)