An Unusual Cation-Binding Site and Distinct Domain–Domain Interactions Distinguish Class II Enolpyruvylshikimate-3-phosphate Synthases-Reference-Cited by-同舟云学术

An Unusual Cation-Binding Site and Distinct Domain–Domain Interactions Distinguish Class II Enolpyruvylshikimate-3-phosphate Synthases

Published:2016-02-12 Issue:8 Volume:55 Page:1239-1245
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Light Samuel H.¹,Krishna Sankar N.¹,Minasov George¹,Anderson Wayne F.¹

Affiliation:

1. Center for Structural Genomics of Infectious Diseases and Department of Biochemistry and Molecular Genetics, Feinberg School of Medicine, Northwestern University, 303 East Chicago Avenue, Chicago, Illinois 60611, United States

Funder

National Institute of Allergy and Infectious Diseases

Advanced Research Projects Agency - Energy

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.5b00553

Reference34 articles.

1. The Shikimate Pathway — A Metabolic Tree with Many Branche

2. 5-Enolpyruvylshikimate-3-phosphate synthase of Klebsiella pneumoniae. 2. Inhibition by glyphosate [N-(phosphononmethyl)glycine]

3. Molecular basis for the herbicide resistance of Roundup Ready crops

4. Structure and topological symmetry of the glyphosate target 5-enolpyruvylshikimate-3-phosphate synthase: a distinctive protein fold.

5. Interaction of the herbicide glyphosate with its target enzyme 5-enolpyruvylshikimate 3-phosphate synthase in atomic detail

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