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1QAP

QUINOLINIC ACID PHOSPHORIBOSYLTRANSFERASE WITH BOUND QUINOLINIC ACID

1QAP の概要
エントリーDOI10.2210/pdb1qap/pdb
分子名称QUINOLINIC ACID PHOSPHORIBOSYLTRANSFERASE, QUINOLINIC ACID (3 entities in total)
機能のキーワードglycosyltransferase, quinolinic acid, nad biosynthesis
由来する生物種Salmonella typhimurium
タンパク質・核酸の鎖数2
化学式量合計65295.44
構造登録者
Eads, J.C.,Ozturk, D.,Wexler, T.B.,Grubmeyer, C.,Sacchettini, J.C. (登録日: 1996-09-20, 公開日: 1997-03-12, 最終更新日: 2024-02-14)
主引用文献Eads, J.C.,Ozturk, D.,Wexler, T.B.,Grubmeyer, C.,Sacchettini, J.C.
A new function for a common fold: the crystal structure of quinolinic acid phosphoribosyltransferase.
Structure, 5:47-58, 1997
Cited by
PubMed Abstract: Quinolinic acid (QA) is a neurotoxin and has been shown to be present at high levels in the central nervous system of patients with certain diseases, such as AIDS and meningitis. The enzyme quinolinic acid phosphoribosyltransferase (QAPRTase) provides the only route for QA metabolism and is also an essential step in de novo NAD biosynthesis. QAPRTase catalyzes the synthesis of nicotinic acid mononucleotide (NAMN) from QA and 5-phosphoribosyl-1-pyrophosphate (PRPP). The structures of several phosphoribosyltransferases (PRTases) have been reported, and all have shown a similar fold of a five-strandard beta sheet surrounded by four alpha helices. A conserved sequence motif of 13 residues is common to these 'type I' PRTases but is not observed in the QAPRTase sequence, suggestive of a different fold for this enzyme.
PubMed: 9016724
DOI: 10.1016/S0969-2126(97)00165-2
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.8 Å)
構造検証レポート
Validation report summary of 1qap
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-22に公開中

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