1IUG

The crystal structure of aspartate aminotransferase which belongs to subgroup IV from Thermus thermophilus

1IUG の概要

• エントリーDOI: 10.2210/pdb1iug/pdb
• 分子名称: putative aspartate aminotransferase, PHOSPHATE ION (3 entities in total)
• 機能のキーワード: wild type, pyridoxal-5'-phosphate form, riken structural genomics/proteomics initiative, rsgi, structural genomics, transferase
• 由来する生物種: Thermus thermophilus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 76718.18

構造登録者

Katsura, Y.,Shirouzu, M.,Yamaguchi, H.,Ishitani, R.,Nureki, O.,Kuramitsu, S.,Hayashi, H.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (登録日: 2002-03-04, 公開日: 2003-11-25, 最終更新日: 2024-12-25)

主引用文献

Katsura, Y.,Shirouzu, M.,Yamaguchi, H.,Ishitani, R.,Nureki, O.,Kuramitsu, S.,Hayashi, H.,Yokoyama, S.
Crystal structure of a putative aspartate aminotransferase belonging to subgroup IV.
Proteins, 55:487-492, 2004

PubMed Abstract: Protein TT0402 from Thermus thermophilus HB8 exhibits about 30-35% sequence identity with proteins belonging to subgroup IV in the aminotransferase family of the fold-type I pyridoxal 5'-phosphate (PLP)-dependent enzymes. In this study, we determined the crystal structure of TT0402 at 2.3 A resolution (R(factor) = 19.9%, R(free) = 23.6%). The overall structure of TT0402 exhibits the fold conserved in aminotransferases, and is most similar to that of the Escherichia coli phosphoserine aminotransferase, which belongs to subgroup IV but shares as little as 13% sequence identity with TT0402. Kinetic assays confirmed that TT0402 has higher transamination activities with the amino group donor, L-glutamate, and somewhat lower activities with L-aspartate. These results indicate that TT0402 is a subgroup IV aminotransferase for the synthesis/degradation of either L-aspartate or a similar compound.

PubMed: 15103612
DOI: 10.1002/prot.20020

実験手法

X-RAY DIFFRACTION (2.2 Å)