Work

Crystal structure of glutamine amidotransferase from Pyrococcus horikoshii OT3

Year: 2005

Type: article

Abstract: 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.)

Source: Proceedings of the Japan Academy Series B

DOI: 10.2183/pjab.81.459

Authors: Shintaro MARUOKA, Woo Cheol LEE, Masayuki KAMO, Norio KUDO, Koji NAGATA, Masaru TANOKURA

Institution: The University of Tokyo

Language: English

Topic: Enzyme Structure and Function

Subfield: Structural Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: bronze

Funders: Ministry of Education, Culture, Sports, Science and Technology, Japan Society for the Promotion of Science, RIKEN

OpenAlex ID: W2014780751

FWCI:

Cites: 21

Cited by: 3

Related to: 10