2EZA

AMINO TERMINAL DOMAIN OF ENZYME I FROM ESCHERICHIA COLI, NMR, RESTRAINED REGULARIZED MEAN STRUCTURE

2EZA の概要

• エントリーDOI: 10.2210/pdb2eza/pdb
• 分子名称: PHOSPHOTRANSFERASE SYSTEM, ENZYME I (1 entity in total)
• 機能のキーワード: phosphotransferase, transferase, kinase, sugar transport
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cytoplasm: P08839
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 28381.32

構造登録者

Clore, G.M.,Tjandra, N.,Garrett, D.S.,Gronenborn, A.M. (登録日: 1997-05-07, 公開日: 1997-08-20, 最終更新日: 2024-05-22)

主引用文献

Tjandra, N.,Garrett, D.S.,Gronenborn, A.M.,Bax, A.,Clore, G.M.
Defining long range order in NMR structure determination from the dependence of heteronuclear relaxation times on rotational diffusion anisotropy.
Nat.Struct.Biol., 4:443-449, 1997

PubMed Abstract: Structure determination by NMR presently relies on short range restraints between atoms in close spatial proximity, principally in the form of short (< 5 A) interproton distances. In the case of modular or multidomain proteins and linear nucleic acids, the density of short interproton distance contacts between structural elements far apart in the sequence may be insufficient to define their relative orientations. In this paper we show how the dependence of heteronuclear longitudinal and transverse relaxation times on the rotational diffusion anisotropy of non-spherical molecules can be readily used to directly provide restraints for simulated annealing structure refinement that characterize long range order a priori. The method is demonstrated using the N-terminal domain of Enzyme I,a protein of 259 residues comprising two distinct domains with a diffusion anisotropy(Dparallel/Dperpendicular)of approximately 2.

PubMed: 9187651
DOI: 10.1038/nsb0697-443

実験手法

SOLUTION NMR