Solution Structure of the 128 kDa Enzyme I Dimer from Escherichia coli and Its 146 kDa Complex with HPr Using Residual Dipolar Couplings and Small- and Wide-Angle X-ray Scattering-Reference-Cited by-同舟云学术

Solution Structure of the 128 kDa Enzyme I Dimer from Escherichia coli and Its 146 kDa Complex with HPr Using Residual Dipolar Couplings and Small- and Wide-Angle X-ray Scattering

Published:2010-08-23 Issue:37 Volume:132 Page:13026-13045
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Schwieters Charles D.¹,Suh Jeong-Yong¹,Grishaev Alexander¹,Ghirlando Rodolfo¹,Takayama Yuki¹,Clore G. Marius¹

Affiliation:

1. Laboratory of Chemical Physics, Building 5, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-0520, Division of Computational Biosciences, Center for Information Technology, National Institutes of Health, Bethesda, Maryland 20892-5624, and Laboratory of Molecular Biology, Building 5, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-0530

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja105485b

Reference77 articles.

1. THE BACTERIAL PHOSPHOENOL-PYRUVATE: GLYCOSE PHOSPHOTRANSFERASE SYSTEM

2. Structure/function studies on the bacterial carbohydrate transporters, enzymes II, of the phosphoenolpyruvate-dependent phosphotransferase system

3. Carbohydrate transporters of the bacterial phosphoenolpyruvate: sugar phosphotransferase system (PTS)

4. How Phosphotransferase System-Related Protein Phosphorylation Regulates Carbohydrate Metabolism in Bacteria

5. Sugar transport by the bacterial phosphotransferase system. Isolation and characterization of enzyme I from Salmonella typhimurium.

Cited by 116 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Elucidation of the Mechanisms of Inter-domain Coupling in the Monomeric State of Enzyme I by High-pressure NMR;Journal of Molecular Biology;2024-05

2. Xplor‐NIH: Better parameters and protocols for NMR protein structure determination;Protein Science;2024-03-19

3. Study of Biomolecular Structure and Dynamics with Xplor-NIH;Residual Dipolar Couplings;2024-02-16

4. NMR Experiments for Measuring RDCs in Biomolecules;Residual Dipolar Couplings;2024-02-16

5. Solution Structure Ensembles of the Open and Closed Forms of the ∼130 kDa Enzyme I via AlphaFold Modeling, Coarse Grained Simulations, and NMR;Journal of the American Chemical Society;2023-06-06