1ZYK

Anthranilate Phosphoribosyltransferase in complex with PRPP, anthranilate and magnesium

1ZYK の概要

• エントリーDOI: 10.2210/pdb1zyk/pdb
• 関連するPDBエントリー: 1GXB 1O17 1XFM 1ZXY
• 分子名称: Anthranilate phosphoribosyltransferase, MAGNESIUM ION, 1-O-pyrophosphono-5-O-phosphono-alpha-D-ribofuranose, ... (5 entities in total)
• 機能のキーワード: anthranilate phosphoribosyltransferase, prpp, anthranilate, trpd, transferase
• 由来する生物種: Sulfolobus solfataricus
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 153329.87

構造登録者

Marino, M.,Deuss, M.,Sterner, R.,Mayans, O. (登録日: 2005-06-10, 公開日: 2006-05-23, 最終更新日: 2023-11-15)

主引用文献

Marino, M.,Deuss, M.,Svergun, D.I.,Konarev, P.V.,Sterner, R.,Mayans, O.
Structural and mutational analysis of substrate complexation by anthranilate phosphoribosyltransferase from Sulfolobus solfataricus.
J.Biol.Chem., 281:21410-21421, 2006

PubMed Abstract: The metabolic synthesis and degradation of essential nucleotide compounds are primarily carried out by phosphoribosyltransferases (PRT) and nucleoside phosphorylases (NP), respectively. Despite the resemblance of their reactions, five classes of PRTs and NPs exist, where anthranilate PRT (AnPRT) constitutes the only evolutionary link between synthesis and degradation processes. We have characterized the active site of dimeric AnPRT from Sulfolobus solfataricus by elucidating crystal structures of the wild-type enzyme complexed to its two natural substrates anthranilate and 5-phosphoribosyl-1-pyrophosphate/Mg(2+). These bind into two different domains within each protomer and are brought together during catalysis by rotational domain motions as shown by small angle x-ray scattering data. Steady-state kinetics of mutated AnPRT variants address the role of active site residues in binding and catalysis. Results allow the comparative analysis of PRT and pyrimidine NP families and expose related structural motifs involved in nucleotide/nucleoside recognition by these enzyme families.

PubMed: 16714288
DOI: 10.1074/jbc.M601403200

実験手法

X-RAY DIFFRACTION (2.4 Å)