The structure of apo tryptophanase fromEscherichia colireveals a wide-open conformation-Reference-Cited by-同舟云学术

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The structure of apo tryptophanase fromEscherichia colireveals a wide-open conformation

Published:2007-08-17 Issue:9 Volume:63 Page:969-974
ISSN:0907-4449
Container-title:Acta Crystallographica Section D Biological Crystallography
language:
Short-container-title:Acta Crystallogr D Biol Cryst

Author:

Tsesin Natalia,Kogan Anna,Gdalevsky Garik Y.,Himanen Juha-Pekka,Cohen-Luria Rivka,Parola Abraham H.,Goldgur Yehuda,Almog Orna

Publisher

International Union of Crystallography (IUCr)

Subject

General Medicine,Structural Biology

Link

http://journals.iucr.org/d/issues/2007/09/00/fw5144/fw5144.pdf

Cited by 13 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. Structural Basis for Allostery in PLP-dependent Enzymes;Frontiers in Molecular Biosciences;2022-04-25

2. Gene Erosion Can Lead to Gain-of-Function Alleles That Contribute to Bacterial Fitness;mBio;2021-08-31

3. The Catalytic Mechanisms of the Reactions between Tryptophan Indole-Lyase and Nonstandard Substrates: The Role of the Ionic State of the Catalytic Group Accepting the Cα Proton of the Substrate;Acta Naturae;2019-09-15

4. The crystal structure of Proteus vulgaris tryptophan indole-lyase complexed with oxindolyl-L-alanine: implications for the reaction mechanism;Acta Crystallographica Section D Structural Biology;2018-07-24

5. A structural view of the dissociation ofEscherichia colitryptophanase;Acta Crystallographica Section D Biological Crystallography;2015-11-26

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