3ZRP

Crystal structure and substrate specificity of a thermophilic archaeal serine : pyruvate aminotransferase from Sulfolobus solfataricus

3ZRP の概要

• エントリーDOI: 10.2210/pdb3zrp/pdb
• 関連するPDBエントリー: 3ZRQ 3ZRR
• 分子名称: SERINE-PYRUVATE AMINOTRANSFERASE (AGXT), PYRIDOXAL-5'-PHOSPHATE (3 entities in total)
• 機能のキーワード: transferase
• 由来する生物種: SULFOLOBUS SOLFATARICUS
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 84551.23

構造登録者

Sayer, C.,Bommer, M.,Isupov, M.N.,Ward, J.,Littlechild, J. (登録日: 2011-06-17, 公開日: 2012-06-27, 最終更新日: 2023-12-20)

主引用文献

Sayer, C.,Bommer, M.,Isupov, M.N.,Ward, J.,Littlechild, J.
Crystal Structure and Substrate Specificity of the Thermophilic Serine:Pyruvate Aminotransferase from Sulfolobus Solfataricus
Acta Crystallogr.,Sect.D, 68:763-, 2012

PubMed Abstract: The three-dimensional structure of the Sulfolobus solfataricus serine:pyruvate aminotransferase has been determined to 1.8 Å resolution. The structure of the protein is a homodimer that adopts the type I fold of pyridoxal 5'-phosphate (PLP)-dependent aminotransferases. The structure revealed the PLP cofactor covalently bound in the active site to the active-site lysine in the internal aldimine form. The structure of the S. solfataricus enzyme was also determined with an amino form of the cofactor pyridoxamine 5'-phosphate bound in the active site and in complex with gabaculine, an aminotransferase inhibitor. These structures showed the changes in the enzyme active site during the course of the catalytic reaction. A comparison of the structure of the S. solfataricus enzyme with that of the closely related alanine:glyoxylate aminotransferase has identified structural features that are proposed to be responsible for the differences in substrate specificity between the two enzymes. These results have been complemented by biochemical studies of the substrate specificity and thermostability of the S. solfataricus enzyme.

PubMed: 22751661
DOI: 10.1107/S0907444912011274

実験手法

X-RAY DIFFRACTION (1.75 Å)