1DJU

CRYSTAL STRUCTURE OF AROMATIC AMINOTRANSFERASE FROM PYROCOCCUS HORIKOSHII OT3

1DJU の概要

• エントリーDOI: 10.2210/pdb1dju/pdb
• 分子名称: AROMATIC AMINOTRANSFERASE, PYRIDOXAL-5'-PHOSPHATE (3 entities in total)
• 機能のキーワード: alpha/beta/alpha, transferase
• 由来する生物種: Pyrococcus horikoshii
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 88181.55

構造登録者

Matsui, I.,Matsui, E.,Sakai, Y.,Kikuchi, H.,Kawarabayashi, H. (登録日: 1999-12-06, 公開日: 2001-04-11, 最終更新日: 2025-03-26)

主引用文献

Matsui, I.,Matsui, E.,Sakai, Y.,Kikuchi, H.,Kawarabayasi, Y.,Ura, H.,Kawaguchi, S.,Kuramitsu, S.,Harata, K.
The molecular structure of hyperthermostable aromatic aminotransferase with novel substrate specificity from Pyrococcus horikoshii.
J.Biol.Chem., 275:4871-4879, 2000

PubMed Abstract: Aromatic amino acid aminotransferase (ArATPh), which has a melting temperature of 120 degrees C, is one of the most thermostable aminotransferases yet to be discovered. The crystal structure of this aminotransferase from the hyperthermophilic archaeon Pyrococcus horikoshii was determined to a resolution of 2.1 A. ArATPh has a homodimer structure in which each subunit is composed of two domains, in a manner similar to other well characterized aminotransferases. By the least square fit after superposing on a mesophilic ArAT, the ArATPh molecule exhibits a large deviation of the main chain coordinates, three shortened alpha-helices, an elongated loop connecting two domains, and a long loop transformed from an alpha-helix, which are all factors that are likely to contribute to its hyperthermostability. The pyridine ring of the cofactor pyridoxal 5'-phosphate covalently binding to Lys(233) is stacked parallel to F121 on one side and interacts with the geminal dimethyl-CH/pi groups of Val(201) on the other side. This tight stacking against the pyridine ring probably contributes to the hyperthermostability of ArATPh. Compared with other ArATs, ArATPh has a novel substrate specificity, the order of preference being Tyr > Phe > Glu > Trp > His>> Met > Leu > Asp > Asn. Its relatively weak activity against Asp is due to lack of an arginine residue corresponding to Arg(292)* (where the asterisk indicates that this is a residues supplied by the other subunit of the dimer) in pig cytosolic aspartate aminotransferase. The enzyme recognizes the aromatic substrate by hydrophobic interaction with aromatic rings (Phe(121) and Tyr(59)*) and probably recognizes acidic substrates by a hydrophilic interaction involving a hydrogen bond network with Thr(264)*.

PubMed: 10671523
DOI: 10.1074/jbc.275.7.4871

実験手法

X-RAY DIFFRACTION (2.1 Å)