2RGW

Catalytic Subunit of M. jannaschii Aspartate Transcarbamoylase

2RGW の概要

• エントリーDOI: 10.2210/pdb2rgw/pdb
• 分子名称: Aspartate carbamoyltransferase, SULFATE ION (3 entities in total)
• 機能のキーワード: aspartate transcarbamoylase, pyrimidine biosynthesis, thermostability, methanococcus jannaschii, transferase
• 由来する生物種: Methanococcus jannaschii
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 211455.85

構造登録者

Vitali, J.,Colaneri, M.J.,Kantrowitz, E.R. (登録日: 2007-10-05, 公開日: 2008-10-14, 最終更新日: 2023-08-30)

主引用文献

Vitali, J.,Colaneri, M.J.,Kantrowitz, E.
Crystal structure of the catalytic trimer of Methanococcus jannaschii aspartate transcarbamoylase.
Proteins, 71:1324-1334, 2008

PubMed Abstract: The catalytic trimer of Methanococcus jannaschii aspartate transcarbamoylase is extremely heat stable, maintaining 75% of its activity after heat treatment for 60 min at 75 degrees C. We undertook its structural analysis in order to understand the molecular basis of its thermostability and gain insight on how its catalytic function adapts to high temperature. Several structural elements potentially contributing to thermostability were identified. These include: (i) changes in the amino acid composition such as a decrease in the thermolabile residues Gln and Asn, an increase in the charged residues Lys and Glu, an increase in Tyr and a decrease in Ala residues; (ii) a larger number of salt bridges, in particular, the improvement of ion-pair networks; (iii) shortening of the N-terminus and shortening of three loops. An interesting feature of the crystal structure is the association of two crystallographically independent catalytic subunits into a staggered complex with an intertrimer distance of 33.8 A. The active site appears similar to Escherichia coli. Upon substrate binding, smaller changes in the global orientation of domains and larger conformational changes of the active site residues are expected as compared to E. coli.

PubMed: 18058907
DOI: 10.1002/prot.21667

実験手法

X-RAY DIFFRACTION (2.8 Å)