1KIJ

Crystal structure of the 43K ATPase domain of Thermus thermophilus gyrase B in complex with novobiocin

1KIJ の概要

• エントリーDOI: 10.2210/pdb1kij/pdb
• 分子名称: DNA GYRASE SUBUNIT B, NOVOBIOCIN, FORMIC ACID, ... (4 entities in total)
• 機能のキーワード: topoisomerase, gyrase b-coumarin complex, isomerase
• 由来する生物種: Thermus thermophilus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 86760.20

構造登録者

Lamour, V.,Hoermann, L.,Jeltsch, J.-M.,Oudet, P.,Moras, D. (登録日: 2001-12-03, 公開日: 2002-06-03, 最終更新日: 2024-02-14)

主引用文献

Lamour, V.,Hoermann, L.,Jeltsch, J.M.,Oudet, P.,Moras, D.
An open conformation of the Thermus thermophilus gyrase B ATP-binding domain.
J.Biol.Chem., 277:18947-18953, 2002

PubMed Abstract: DNA gyrase forms an A(2)B(2) tetramer involved in DNA replication, repair, recombination, and transcription in which the B subunit catalyzes ATP hydrolysis. The Thermus thermophilus and Escherichia coli gyrases are homologues and present the same catalytic activity. When compared with that of the E. coli 43K-5'-adenylyl-beta,gamma-imidodiphosphate complex, the crystal structure of Gyrase B 43K ATPase domain in complex with novobiocin, one of the most potent inhibitors of gyrase shows large conformational changes of the subdomains within the dimer. The stabilization of loop 98-118 closing the active site through dimeric contacts and interaction with domain 2 allows to observe novobiocin-protein interactions that could not be seen in the 24K-inhibitor complexes. Furthermore, this loop adopts a position which defines an "open" conformation of the active site in absence of ATP, in contrast with the "closed" conformation adopted upon ATP binding. All together, these results indicate how the subdomains may propagate conformational changes from the active site and provide crucial information for the design of more specific inhibitors.

PubMed: 11850422
DOI: 10.1074/jbc.M111740200

実験手法

X-RAY DIFFRACTION (2.3 Å)