Crystal structure of glutamine amidotransferase from Pyrococcus horikoshii OT3

Crystal structure of glutamine amidotransferase from Pyrococcus horikoshii OT3

Glutamine amidotransferases (GATases) hydrolyze glutamine and generate ammonia. The glutamine amide nitrogen is utilized for the biosynthesis of a variety of molecules such as amino acids, coenzymes, antibiotics, purine and pyrimidine nucleotides, and glucosamine. Here, we determined the crystal str...

Full description

Saved in:
Bibliographic Details
Published in:Proceedings of the Japan Academy, Series B Vol. 81; no. 10; pp. 459 - 462
Main Authors: MARUOKA, Shintaro, LEE, Woo Cheol, KAMO, Masayuki, KUDO, Norio, NAGATA, Koji, TANOKURA, Masaru
Format: Journal Article
Language:English
Published: The Japan Academy 01-01-2005
Subjects:
Escherichia coli
Glutamine amidotransferase
protein structure
Pyrococcus horikoshii
Sulfolobus solfataricus
X-ray crystallography
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Glutamine amidotransferases (GATases) hydrolyze glutamine and generate ammonia. The glutamine amide nitrogen is utilized for the biosynthesis of a variety of molecules such as amino acids, coenzymes, antibiotics, purine and pyrimidine nucleotides, and glucosamine. Here, we determined the crystal structure of a GATase (PH1346) from the hyperthermophilic archaeon Pyrococcus horikoshii OT3 at 1.89 Å resolution. Its overall structure and active site are the most similar to those of E. coli guanosine 5'-monophosphate (GMP) synthase and Sulfolobus solfataricus anthranilate synthase, respectively. (Communicated by Masanori OTSUKA, M.J.A.)
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0386-2208
1349-2896
DOI:10.2183/pjab.81.459