A novel crystal form of pyrrolysyl-tRNA synthetase reveals the pre- and post-aminoacyl-tRNA synthesis conformational states of the adenylate and aminoacyl moieties and an asparagine residue in the catalytic site-Reference-Cited by-同舟云学术

A novel crystal form of pyrrolysyl-tRNA synthetase reveals the pre- and post-aminoacyl-tRNA synthesis conformational states of the adenylate and aminoacyl moieties and an asparagine residue in the catalytic site

Published:2012-12-20 Issue:1 Volume:69 Page:5-15
ISSN:0907-4449
Container-title:Acta Crystallographica Section D Biological Crystallography
language:
Short-container-title:Acta Crystallogr D Biol Cryst

Author:

Yanagisawa Tatsuo,Sumida Tomomi,Ishii Ryohei,Yokoyama Shigeyuki

Publisher

International Union of Crystallography (IUCr)

Subject

General Medicine,Structural Biology

Link

http://journals.iucr.org/d/issues/2013/01/00/be5210/be5210.pdf

Reference53 articles.

1. Crystal Structure Analysis of the Activation of Histidine by Thermus thermophilus Histidyl-tRNA Synthetase,

2. Glycyl-tRNA synthetase uses a negatively charged pit for specific recognition and activation of glycine 1 1Edited by R. Huber

3. Crystal structure of histidyl-tRNA synthetase from Escherichia coli complexed with histidyl-adenylate.

4. Crystal Structures at 2.5 Angstrom Resolution of Seryl-tRNA Synthetase Complexed with Two Analogs of Seryl Adenylate

5. Structure of the unusual seryl-tRNA synthetase reveals a distinct zinc-dependent mode of substrate recognition

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