4ADC

Structural and functional study of succinyl-ornithine transaminase from E. coli

4ADC の概要

• エントリーDOI: 10.2210/pdb4adc/pdb
• 関連するPDBエントリー: 4ADB 4ADD 4ADE
• 分子名称: SUCCINYLORNITHINE TRANSAMINASE, PYRIDOXAL-5'-PHOSPHATE, SODIUM ION, ... (5 entities in total)
• 機能のキーワード: transferase, plp enzymes, aminotransferase
• 由来する生物種: ESCHERICHIA COLI
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 175907.68

構造登録者

Newman, J.,Peat, T.S. (登録日: 2011-12-23, 公開日: 2013-01-16, 最終更新日: 2023-12-20)

主引用文献

Newman, J.,Seabrook, S.,Surjadi, R.,Williams, C.C.,Lucent, D.,Wilding, M.,Scott, C.,Peat, T.S.
Determination of the Structure of the Catabolic N-Succinylornithine Transaminase (Astc) from Escherichia Coli.
Plos One, 8:58298-, 2013

PubMed Abstract: Escherichia coli possesses two acyl ornithine aminotransferases, one catabolic (AstC) and the other anabolic (ArgD), that participate in L-arginine metabolism. Although only 58% identical, the enzymes have been shown to be functionally interchangeable. Here we have purified AstC and have obtained X-ray crystal structures of apo and holo-AstC and of the enzyme complexed with its physiological substrate, succinylornithine. We compare the structures obtained in this study with those of ArgD from Salmonella typhimurium obtained elsewhere, finding several notable differences. Docking studies were used to explore the docking modes of several substrates (ornithine, succinylornithine and acetylornithine) and the co-substrate glutamate/α-ketogluterate. The docking studies support our observations that AstC has a strong preference for acylated ornithine species over ornithine itself, and suggest that the increase in specificity associated with acylation is caused by steric and desolvation effects rather than specific interactions between the substrate and enzyme.

PubMed: 23484010
DOI: 10.1371/JOURNAL.PONE.0058298

実験手法

X-RAY DIFFRACTION (2.3 Å)