1ZID

LONG FATTY ACID CHAIN ENOYL-ACP REDUCTASE (INHA) IN COMPLEX WITH AN ISONICOTINIC-ACYL-NADH INHIBITOR

1ZID の概要

• エントリーDOI: 10.2210/pdb1zid/pdb
• 分子名称: ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE, ISONICOTINIC-ACETYL-NICOTINAMIDE-ADENINE DINUCLEOTIDE (3 entities in total)
• 機能のキーワード: oxidoreductase, inha enzyme, isoniazid, modified nadh, enoyl-acp reductase, tuberculosis, mycolic acid biosynthesis, structural genomics, psi, protein structure initiative, tb structural genomics consortium, tbsgc
• 由来する生物種: Mycobacterium tuberculosis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 29162.08

構造登録者

Rozwarski, D.A.,Jacobs Jr., W.R.,Sacchettini, J.C.,TB Structural Genomics Consortium (TBSGC) (登録日: 1997-03-25, 公開日: 1998-03-25, 最終更新日: 2024-05-22)

主引用文献

Rozwarski, D.A.,Grant, G.A.,Barton, D.H.,Jacobs Jr., W.R.,Sacchettini, J.C.
Modification of the NADH of the isoniazid target (InhA) from Mycobacterium tuberculosis.
Science, 279:98-102, 1998

PubMed Abstract: The preferred antitubercular drug isoniazid specifically targets a long-chain enoyl-acyl carrier protein reductase (InhA), an enzyme essential for mycolic acid biosynthesis in Mycobacterium tuberculosis. Despite the widespread use of this drug for more than 40 years, its precise mode of action has remained obscure. Data from x-ray crystallography and mass spectrometry reveal that the mechanism of isoniazid action against InhA is covalent attachment of the activated form of the drug to the nicotinamide ring of nicotinamide adenine dinucleotide bound within the active site of InhA.

PubMed: 9417034
DOI: 10.1126/science.279.5347.98

実験手法

X-RAY DIFFRACTION (2.7 Å)